Aminoacyl tRNA Synthetase: Difference between revisions

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'''Aminoacyl tRNA synthetase''' (aaRS) catalyzes the esterification of a specific amino acid to its cognate tRNA to form an aminoacyl-tRNA.  The amino acid is transferred by the ribosome from the aminoacylated-tRNA onto a growing polypeptide chain.  Class I of aaRS is a monomer or dimer, it has 2 highly conserved sequence motifs and it aminoacylates at the 2’-OH of an adenosine nucleotide. Class II of aaRS is a dimer or tetramer, it has 3 highly conserved sequence motifs and it aminoacylates at the 3’-OH of an adenosine nucleotide.  CP1 domain of RS edits a mischarged aa-tRNA.  Some of the crystal structures are complexes of the RS with their reactant analog: amino acid-sulfamoyl adenine (aa-SA).  
'''Aminoacyl tRNA synthetase''' (aaRS) catalyzes the esterification of a specific amino acid to its cognate tRNA to form an aminoacyl-tRNA.  The amino acid is transferred by the ribosome from the aminoacylated-tRNA onto a growing polypeptide chain.  Class I of aaRS is a monomer or dimer, it has 2 highly conserved sequence motifs and it aminoacylates at the 2’-OH of an adenosine nucleotide. Class II of aaRS is a dimer or tetramer, it has 3 highly conserved sequence motifs and it aminoacylates at the 3’-OH of an adenosine nucleotide.  CP1 domain of RS edits a mischarged aa-tRNA.  Some of the crystal structures are complexes of the RS with their reactant analog: amino acid-sulfamoyl adenine (aa-SA). For '''pyrrolysyl-RS''' details see [[Pyrrolysyl-tRNA synthetase]].




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**[[1h4q]] - TtProRS + Pro-tRNA + Pro-ol<br />
**[[1h4q]] - TtProRS + Pro-tRNA + Pro-ol<br />
**[[1h4s]] - TtProRS + Pro-tRNA + Pro-SA<br />
**[[1h4s]] - TtProRS + Pro-tRNA + Pro-SA<br />
*'''Pyrrolysyl-RS'''
**[[2e3c]] - MmPylRS catalytic domain <br />
**[[3vqw]], [[3vqx]], [[4cs2]] - MmPylRS catalytic domain (mutant)<br />
**[[3dsq]] – DhPylRS <br />
*''Pyrrolysyl-RS binary complex''
**[[3qtc]] – MmPylRS catalytic domain (mutant) + AMP-ATP analog<br />
**[[2q7e]] - MmPylRS catalytic domain + ATP analog<br />
**[[2zcd]] - MmPylRS catalytic domain + AMP-ATP analog<br />
**[[3vqv]] - MmPylRS catalytic domain + AMPPNP <br />
**[[2zni]] – DhPylRS + tRNA <br />
**[[4ch3]], [[4ch4]], [[4ch5]], [[4ch6]] - MmPylRS catalytic domain + adenylated lysine derivative<br />
**[[4cs3]] - MmPylRS catalytic domain (mutant) + adenylated lysine derivative<br />
*''Pyrrolysyl-RS ternary complex''
**[[2zce]] - MmPylRS catalytic domain + pyrrolysine + ATP analog<br />
**[[2q7g]] - MmPylRS catalytic domain + pyrrolysine analog + ATP<br />
**[[2zim]], [[2q7h]] - MmPylRS catalytic domain + adenylated pyrrolysine + pyrophosphate<br />
**[[2zio]] - MmPylRS catalytic domain + AlocLys-AMP + ATP analog<br />
**[[3vqy]] - MmPylRS catalytic domain + butoxycarbonyl lysine + AMPPNP <br />
**[[4q6g]] - MmPylRS catalytic domain + acetyl lysine + ADPNP <br />
**[[4tqd]] - MmPylRS catalytic domain + iodo-Phe + ATP <br />
**[[4tqf]] - MmPylRS catalytic domain + bromothienylo-Ala + ATP <br />
**[[2zin]] - MmPylRS catalytic domain + butoxycarbonyl lysine + ATP analog <br />


*'''Ser-RS'''
*'''Ser-RS'''

Revision as of 13:58, 25 May 2015

File:3l4g.png
Crystal Structure of Aminoacyl tRNA synthetase 3l4g

Template:STRUCTURE 1f7v














Aminoacyl tRNA synthetase (aaRS) catalyzes the esterification of a specific amino acid to its cognate tRNA to form an aminoacyl-tRNA. The amino acid is transferred by the ribosome from the aminoacylated-tRNA onto a growing polypeptide chain. Class I of aaRS is a monomer or dimer, it has 2 highly conserved sequence motifs and it aminoacylates at the 2’-OH of an adenosine nucleotide. Class II of aaRS is a dimer or tetramer, it has 3 highly conserved sequence motifs and it aminoacylates at the 3’-OH of an adenosine nucleotide. CP1 domain of RS edits a mischarged aa-tRNA. Some of the crystal structures are complexes of the RS with their reactant analog: amino acid-sulfamoyl adenine (aa-SA). For pyrrolysyl-RS details see Pyrrolysyl-tRNA synthetase.


3D Structures of Aminoacyl tRNA synthetase3D Structures of Aminoacyl tRNA synthetase

Updated on 25-May-2015

  • Glu-RS + small substrates or analogs
    • 3afh - TmGluRS + Glu-AMP analog
    • 2rd2, 2re8 – EcGluRS (mutant) + Glu-SA
    • 2cuz – TtGluRS + Glu
    • 1j09 - TtGluRS + Glu + ATP
    • 1n75 - TtGluRS + ATP
    • 2fco - GluRS residues 2-485 + Glu – Synechococcus elongatus
  • Glu-RS + tRNA
    • 1zjw – EcGluRS + Glu-tRNA
  • Glu-RS ternary complex
    • 3akz, 3al0 – TmGluRS + tRNA + Glu-AMP analog – Thermotoga maritima
    • 1o0b, 1o0c - EcGluRS + Glu-tRNA + Glu + AMP
      2cv0, 1n77 - TtGluRS + Glu + Glu-tRNA
    • 1n78 - TtGluRS + Glu-ol + Glu-tRNA
    • 2cv1 - TtGluRS + Glu-ol + ATP + Glu-tRNA
    • 2cv2 - TtGluRS + Glu-SA + Glu-tRNA
    • 2hrk, 2hsm - yGluRS N-terminal + GU4 nucleic-binding protein 1
  • Ile-RS
  • Ile-RS + small substrates or analogs
    • 1ue0 - TtIleRS editing domain + Val
    • 1wnz - TtIleS editing domain + Val-adenylate
    • 1wk8 - TtIleRS editing domain + Val-SA
    • 1jzq – TtIleS + Ile-adenylate analog
    • 1jzs – TtIleS + antibiotic
  • Ile-RS ternary complex
    • 1ffy, 1qu2, 1qu3 - SaIleRS + Ile-tRNA + antibiotic - Staphylococcus aureus
  • Leu-RS
    • 3o0a – AaLeuRS hydrolytic domain – Aquifex aeolicus
      2wfd – hLeuRS editing domain – human
    • 2wfe - CaLeuRS editing domain – Candida albicans
    • 2ajg - EcLeuRS editing domain
    • 1wkb – PhLeuRS residues 1-810
  • Leu-RS + small substrates or analogs
    • 2wfg - CaLeuRS editing domain + benzoxaborole-AMP
    • 2v0c – TtLeuRS + Leu-SA + benzoxaborole-AMP
    • 1h3n - TtLeuRS + Leu-SA
    • 1obc, 1obh – TtLeuRS + substrate analog
    • 2ajh, 2aji - EcLeuRS editing domain + aa
  • Leu-RS + tRNA
    • 1wz2 – PhLeuRS Leu-tRNA
  • Leu-RS ternary complex
    • 2v0g - TtLeuRS + Leu-tRNA + benzoxaborole-AMP
    • 2bte, 2byt - TtLeuRS + Leu-tRNA + Leu
  • Lys-RS
    • 1irx – PhLysRS
    • 1bbw – EcLysRS
    • 1krs, 1krt – EcLysRS anticodon-binding domain – NMR
      3dsq – DhLysRS – Desulfitobacterium hafniense
    • 2e3c - MmLysRS catalytic domain - Methanosarcina mazei
    • 3bju – hLysRS residues 70-579
  • Lys-RS + small substrates or analogs
    • 3a74 – GsLysRS + diadenosine tetraphosphate – Geobacillus stearothermophilus
    • 3e9h, 3e9i – BsLysRS + Lys-SA - Bacillus stearothermophilus
    • 2zin – MmLysRS catalytic domain + Boc-Lys + ATP analog
    • 2zio - MmLysRS catalytic domain + Aloc-Lys-AMP + PNP
    • 2zcd - MmLysRS catalytic domain + AMPPNP
    • 2zce - MmLysRS catalytic domain + pyrro-Lys + ATP analog
    • 2zim - MmLysRS residues 185-454+ pyrro-Lys-adenylate
    • 2q7e - MmLysRS C-terminal + ATP analog
    • 2q7g - MmLysRS C-terminal+ pyrro-Lys analog+ ATP
    • 1bbu, 1e10, 1lyl – EcLysRS + Lys
    • 1e1t - EcLysRS + Lys-adenylate
    • 1e22 - EcLysRS + Lys + AMPPCP
    • 1e24 - EcLysRS + Lys + ATP
  • Lys-RS + tRNA
  • Met-RS
    • 1a8h – TtMetRS
    • 1med, 1mea – EcMetRS Zinc-binding domain - NMR
    • 1qqt - EcMetRS residues 2-552
    • 2x1l - MsMetRS residues 2-515 – Mycobacterium smegmatis
    • 3h97 – EcMetRS residues 2-548 (mutant)
    • 3h9c - EcMetRS residues 2-548
    • 2d54, 2d5b – TtMetRS (mutant)
    • 1woy – TtMetRS residues 1-500 (mutant)
    • 2djv – hMetRS WHEP-TRS domain – NMR
    • 1pyb – AaMetRS β subunit
    • 1rqg – PaMetRS – Pyrococcus abyssi
    • 1mkh – PaMetRS C-terminal
  • Met-RS + small substrates or analogs
    • 3kfl – LmMetRS residues 206-747+ Met-adenylate - Leishmania major
    • 2x1m - MsMetRS residues 2-515 + Met
    • 1p7p, 1pfu, 1pfv, 1pfw - EcMetRS residues 2-548 + Met
    • 1pfy - EcMetRS residues 1-551 + Met-SA
    • 1f4l - EcMetRS residues 1-551 + Met
    • 1pg0 - EcMetRS residues 1-551 + Met-adenylate
    • 1pg2 - EcMetRS residues 1-551 + Met + adenine
    • 3h99 - EcMetRS residues 2-548 (mutant) + Met
    • 3h9b - EcMetRS residues 2-548 (mutant) + azidonorleucine
    • 4dlp - MetRS + SMet – Brucella melitensis
  • Met-RS + tRNA
    • 2csx – AaMetRS + Met-tRNA
  • Met-RS + tRNA
    • 2ct8 - AaMetRS + Met-tRNA + Met-SA
    • 2dxi – TtMetRS + tRNA + ATP + Glu-ol
  • Met-RS coplex
    • 4bl7, 4bvx, 4bvy - hMetRS N-terminal + elongation factor P18
    • 2hsn - yMetRS N-terminal + GU4 nucleic-binding protein 1 N-terminal
  • Trp-RS
    • 1d2r - GsTrpRS
    • 3prh – TrpRS (mutant) – Bacillus subtilis
    • 3n9i – TrpRS – Yarsinia pestis
    • 3m5w – CjTrpRS – Campylobacter jejuni
    • 3a04 – ApTrpRS – Aeropyrum pernix
    • 3hzr – EhTrpRS – Entamoeba histolytica
    • 3i05 – TbTrpRS residues 3-389 – Trypanosoma brucei
    • 3hv0 – TRrpS residues 206-593 – Cryptosporidium parvum
    • 3foc – GlTrpRS – Giardia lamblia
    • 1o5t – hTrpRS catalytic fragment
    • 1ulh – hTrpRS residues 35-424
    • 2el7 – TtTrpRS
    • 2ip1, 3kt0 – yTrpRS – yeast
    • 2yy5 – TrpRS – Mycoplasma pneumoniae
    • 2g36 – TmTrpRS
    • 1bks – StTrpRS + pyridoxal phosphate
  • Trp-RS + small substrates or analogs
    • 3a05 – ApTrpRS + Trp
    • 3kt3 – yTrpRS + Trp-adenylate
    • 3kt6, 3kt8 – yTrpRS + Trp
    • 3jxe – PhTrpRS + Trp-adenylate
    • 3fhj, 3fio – BsTrpRS + Trp + AMP + Pi
    • 2quh – hTrpRS + Trp
    • 2qui - hTrpRS + Trp-amide + ATP
    • 2quj - hTrpRS + Trp-adenylate
    • 2quk – hTrpRS + ATP
    • 2ov4 – GsTrpRS + adenosine tetraphosphate
    • 1i6k, 1i6l, 1i6m – GsTrpRS + Trp-adenylate
    • 1yid, 2a4m – DrTrpRS + ATP
    • 1yi8, 1yia – DrTrpRS + Trp
    • 1mau – GsTrpRS + Trp + ATP
    • 1maw, 1m83 - GsTrpRS + ATP
    • 1mb2 - GsTrpRS + Trp
    • 3tze - TrpRS + Trp - Encephalitozoon cuniculi
    • 3tzl - CjTrpRS + Trp + ADP
    • 3sz3 - TrpRS + Trp - Vibrio cholerae
  • Trp-RS + tRNA
  • Tyr-RS
  • Tyr-RS + small substrates or analogs
    • 3ts1 – GsTyrRS + Tyr-adenylate intermediate
    • 4ts1 – GsTyrRS + Tyr
    • 3p0h, 3p0i, 3p0j – LmTyrRS + inhibitor
    • 3n2y – MjTyrRS + tetrazolyl phenylalanine
    • 2zp1 – MjTyrRS (mutant) + Tyr
    • 1zh0 - MjTyrRS (mutant) + naphthyl-Ala
    • 1zh6 - MjTyrRS (mutant) + acetyl-Phe
    • 2ag6 - MjTyrRS (mutant) + bromo-Phe
    • 4hjx - MjTyrRS (mutant) + di-fluoro-Tyr
    • 2yxn – EcTyrRS residues 1-322 + azido-Tyr
    • 1vbm – EcTyrRS + Tyr-SA
    • 1vbn – EcTyrRS (mutant) + Tyr-SA
    • 1wq3, 1wq4 - EcTyrRS (mutant) + Tyr
    • 1x8x – EcTyrRS + Tyr
    • 2pid – hTyrRS residues 28-375 + Tyr-SA
    • 2j5b – TyrRS residues 2-346 + Tyr-ol – Acanthamoeba polyphaga minivirus
    • 2dlc – yTyrRS + tRNA + Tyr-SA
    • 2cyb – AfTyrRS + Tyr - Archaeoglobus fulgidus
    • 2cyc – PhTyrRS + Tyr
    • 1q11 – hTyrRS residues 1-364 + Tyr-ol
    • 1h3e - TtTyrRS + Tyr-tRNA + Tyr-ol + ATP
    • 1h3f - TtTyrRS + Tyr-ol
    • 1jh3 – GsTyrRS C-terminal – NMR
    • 1jii, 1jij, 1jil, 1jik – SaTyrRS + inhibitor
  • Tyr-RS + tRNA
    • 1j1u – MjTyrRS + Tyr-tRNA
    • 2rkj – NcTyrRS + RNA
  • Val-RS
  • Val-RS ternary complex
    • 1ivs – TtValRS + Val-SA + Val-tRNA
    • 1gax - TtValRS + Val-adenylate analog + Val-tRNA
  • Class II aaRS
  • Ala-RS
  • Ala-RS + small substrates or analogs
    • 3hxu, 3hxv, 3hxw – EcAlaRS catalytic fragment + aa-adenylate
    • 3hxz, 3hy0, 3hy1 - EcAlaRS catalytic fragment (mutant) + aa-adenylate
    • 3hxx - EcAlaRS catalytic fragment + AMPPCP
    • 3hxy - EcAlaRS catalytic fragment + AMPPCP + Ala-AMP + PCP
    • 3htz - AaAlaRS residues 2-454 + Ser
    • 1yfr – AaAlaRS + ATP
    • 1yfs – AaAlaRS + Ala
    • 1yft, 1ygb - AaAlaRS catalytic fragment + aa
    • 2zzg - PhAlaRS + Ala-SA<br /
    • 2ztg – AfAlaRS + Ala-SA
  • Asp-RS
  • Asp-RS + small substrates or analogs
    • 3nel – TkAspRS + Asp
    • 3nem - TkAspRS + Asp-adenylate
  • Asp-RS + tRNA
  • Asp-RS ternary complex
    • 1il2, 1c0a – EcAspRS + Asp-tRNA + Asp-adenylate
  • Asn-RS
    • 1x56 - PhAsnRS
    • 2kqr – BmAsnRS N-terminal – NMR – Brugia malayi
  • Asn-RS + small substrates or analogs
    • 2xti – BmAsnRS catalytic fragment + Asn-adenine analog
    • 2xgt - BmAsnRS catalytic fragment + Asn-SA
    • 1x54 – PhAsnRS + Asn-adenylate
    • 1x55 - PhAsnRS + Asn-SA
    • 11as – EcAsnRS + Asn
    • 12as - EcAsnRS + Asn + AMP
  • Gly-RS
    • 1ati – TtGlyRS
    • 2q5h – hGlyRS residues 55-739
    • 2q5i - hGlyRS residues 55-739 (mutant)
    • 2pme – hGlyRS
    • 2pmf – hGlyRS (mutant)
    • 1j5w – TmGlyRS α chain
  • Gly-RS + small substrates or analogs
    • 2zt5, 2zxf – hGlyRS residues 55-739 + bis-adenosine tetraphosphate
    • 2zt6 - hGlyRS residues 55-739 + AMPCPP
    • 2zt7 - hGlyRS residues 55-739 + Gly + ATP
    • 2zt8 - hGlyRS residues 55-739 + Gly-AMP analog
    • 1b76 – TtGlyRS + ATP
    • 1ggm – TtGlyRS + Gly-adenylate
  • His-RS
    • 3net – HisRS – Nostoc
    • 1h4v – TtHisRS
    • 1qe0 – SaHisRS
    • 3hri – TbHisRS
    • 1x59 – hHisRS WHEP-TRS domain - NMR
  • His-RS + small substrates or analogs
    • 3lc0 – HisRS residues 45-478 + His – Trypanosoma cruzi
    • 1adj – TtHisRS + His
    • 3hrk - TbHisRS + His-adenylate
    • 2el9 - EcHisRS + His-SA
    • 1kmm, 1ady - EcHisRS + His-adenylate
    • 1kmn - EcHisRS + His-ol + ATP
  • Phe-RS
    • 1pys – TtPheRS
    • 3l4g, 3cmq – hPheRS
    • 2cxi – PhPheRS β chain N-terminal
      3ica – PheRS β chain – Porphyromonas gingivalis
  • Phe-RS + small substrates or analogs
    • 3pco – EcPheRS + phenylalanine+ AMP
    • 3hfz, 2amc – TtPheRS α+β chains + Tyr
    • 2akw, 1b70 - TtPheRS α+β chains + Phe
    • 1jjc, 1b7y - TtPheRS α+β chains + Phe-adenylate
    • 2aly - TtPheRS α+β chains + Phe-SA
    • 2rhq, 2rhs – PheRS α+β chains (mutant) + inhibitor – Staphylococcus haemolyticus
  • Phe-RS + tRNA
    • 1eiy - TtPheRS α+β chains + Phe-tRNA
  • Phe-RS ternary complex
    • 2iy5 - TtPheRS α+β chains + Phe-ol + Phe-tRNA
  • Pro-RS
    • 1hc7 – TtProRS
    • 2i4l – RpProRS – Rhodopseudomonas palustris
    • 1nj2 - MtProRS – Methanothermobacter thermautotrophicus
    • 1nj8 – MjProRS
  • Pro-RS + small substrates or analogs
    • 3ial – GlProRS residues 34-542 + Pro-adenylate
    • 2i4m, 2i4n – RpProRS + aa-SA
    • 2i4o – RpProRS + ATP
    • 2j3l – EfProRS + Pro-SA – Enterococcus faecalis
    • 2j3m – EfProRS + Pro-ol + ATP
    • 1nj1, 1nj5, 1nj6 – MtProRS + aa-SA
    • 1h4t - TtProRS + Pro
  • Pro-RS ternary complex
    • 1h4q - TtProRS + Pro-tRNA + Pro-ol
    • 1h4s - TtProRS + Pro-tRNA + Pro-SA
  • Pyrrolysyl-RS
    • 2e3c - MmPylRS catalytic domain
    • 3vqw, 3vqx, 4cs2 - MmPylRS catalytic domain (mutant)
    • 3dsq – DhPylRS
  • Pyrrolysyl-RS binary complex
    • 3qtc – MmPylRS catalytic domain (mutant) + AMP-ATP analog
    • 2q7e - MmPylRS catalytic domain + ATP analog
    • 2zcd - MmPylRS catalytic domain + AMP-ATP analog
    • 3vqv - MmPylRS catalytic domain + AMPPNP
    • 2zni – DhPylRS + tRNA
    • 4ch3, 4ch4, 4ch5, 4ch6 - MmPylRS catalytic domain + adenylated lysine derivative
    • 4cs3 - MmPylRS catalytic domain (mutant) + adenylated lysine derivative
  • Pyrrolysyl-RS ternary complex
    • 2zce - MmPylRS catalytic domain + pyrrolysine + ATP analog
    • 2q7g - MmPylRS catalytic domain + pyrrolysine analog + ATP
    • 2zim, 2q7h - MmPylRS catalytic domain + adenylated pyrrolysine + pyrophosphate
    • 2zio - MmPylRS catalytic domain + AlocLys-AMP + ATP analog
    • 3vqy - MmPylRS catalytic domain + butoxycarbonyl lysine + AMPPNP
    • 4q6g - MmPylRS catalytic domain + acetyl lysine + ADPNP
    • 4tqd - MmPylRS catalytic domain + iodo-Phe + ATP
    • 4tqf - MmPylRS catalytic domain + bromothienylo-Ala + ATP
    • 2zin - MmPylRS catalytic domain + butoxycarbonyl lysine + ATP analog
  • Ser-RS
    • 3lsq – TbSerRS
    • 1sry - TtSerRS
    • 3err – TtSerRS/dynein heavy chain
    • 2zr3 – PhSerRS
    • 2dq3 – AaSerRS
    • 2du7 – MjSerRS
    • 2odr – SerRS – Methanococcus maripaludis
    • 2cim – MbSerRS – Methanosarcina barkeri
    • 1wle – SerRS – bovine
  • Ser-RS + small substrates or analogs
    • 2zr2 – PhSerRS + ATP
    • 2cj9 – MbSerRS + Ser-SA
    • 2cjb – MbSerRS + Ser
    • 2cja – MbSerRS + ATP
    • 1ses, 1set – TtSerRS + Ser-adenylate analog
    • 3lss – TbSerRS + ATP
  • Ser-RS + tRNA
    • 1ser – TtSerRS + Ser-tRNA
    • 2du4 - AfSerRS + Cys-tRNA
  • Ser-RS ternary complex
    • 2du3 – AfSerRS + Cys-tRNA + phosphoserine
    • 2du5, 2du6 - AfSerRS (mutant) + Cys-tRNA + phosphoserine
  • Thr-RS
    • 1y2q - PaThrRS editing domain
    • 1wwt – hThrRS TGS domain – NMR
    • 1tje - EcThrRS editing domain
  • Thr-RS + small substrates or analogs
    • 3pd2, 3pd3, 3pd4, 3pd5 – PaThrRS editing domain + aa-aminoadenosine
    • 2hkz – PaThrRS editing domain + Ser
    • 2hl0, 2hl1 - PaThrRS editing domain + Ser-adenylate
    • 2hl2 - PaThrRS editing domain + Ser-SA
    • 1tke - EcThrRS editing domain + Ser
    • 1tkg - EcThrRS editing domain + Ser-SA
    • 1tky - EcThrRS editing domain + Ser-adenylate
    • 1fyf, 1evl - EcThrRS catalytic and anticodon-binding domains + aa-SA
    • 1evk - EcThrRS catalytic and anticodon-binding domains + Thr
    • 1nyq – SaThrRS + Thr-SA
    • 1nyr – SaThrRS + ATP
  • Thr-RS + tRNA
    • 1qf6 – EcThrRS + Thr-tRNA
    • 1kog – EcThrRS catalytic and anticodon-binding domains + mRNA
  • Multifunctional RS

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman, Ann Taylor