2iy5: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2iy5.gif|left|200px]]<br /><applet load="2iy5" size=" | [[Image:2iy5.gif|left|200px]]<br /><applet load="2iy5" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2iy5, resolution 3.10Å" /> | caption="2iy5, resolution 3.10Å" /> | ||
'''PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH TRNA AND A PHENYLALANYL-ADENYLATE ANALOG'''<br /> | '''PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH TRNA AND A PHENYLALANYL-ADENYLATE ANALOG'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
2IY5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with MG and FYA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phenylalanine--tRNA_ligase Phenylalanine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.20 6.1.1.20] Known structural/functional Site: <scene name='pdbsite=AC1:Mg Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http:// | 2IY5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=FYA:'>FYA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phenylalanine--tRNA_ligase Phenylalanine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.20 6.1.1.20] Known structural/functional Site: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IY5 OCA]. | ||
==Reference== | ==Reference== | ||
| Line 37: | Line 37: | ||
[[Category: trna-binding]] | [[Category: trna-binding]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:39:36 2008'' | ||
Revision as of 11:39, 3 February 2008
|
PHENYLALANYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH TRNA AND A PHENYLALANYL-ADENYLATE ANALOG
OverviewOverview
The crystal structure of the ternary complex of (alphabeta)(2), heterotetrameric phenylalanyl-tRNA synthetase (PheRS) from Thermus, thermophilus with cognate tRNA(Phe) and a nonhydrolyzable, phenylalanyl-adenylate analogue (PheOH-AMP) has been determined at 3.1 A, resolution. It reveals conformational changes in tRNA(Phe) induced by the, PheOH-AMP binding. The single-stranded 3' end exhibits a hairpin, conformation in contrast to the partial unwinding observed previously in, the binary PheRS.tRNA(Phe) complex. The CCA end orientation is stabilized, by extensive base-specific interactions of A76 and C75 with the protein, and by intra-RNA interactions of A73 with adjacent nucleotides. The, 4-amino group of the "bulged out" C75 is trapped by two negatively charged, residues of the beta subunit (Glubeta31 and Aspbeta33), highly conserved, in eubacterial PheRSs. The position of the A76 base is stabilized by, interactions with Hisalpha212 of motif 2 (universally conserved in PheRSs), and class II-invariant Argalpha321 of motif 3. Important conformational, changes induced by the binding of tRNA(Phe) and PheOH-AMP are observed in, the catalytic domain: the motif 2 loop and a "helical" loop (residues, 139-152 of the alpha subunit) undergo coordinated displacement;, Metalpha148 of the helical loop adopts a conformation preventing the 2'-OH, group of A76 from approaching the alpha-carbonyl carbon of PheOH-AMP. The, unfavorable position of the terminal ribose stems from the absence of the, alpha-carbonyl oxygen in the analogue. Our data suggest that the, idiosyncratic feature of PheRS, which aminoacylates the 2'-OH group of the, terminal ribose, is dictated by the system-specific topology of the CCA, end-binding site.
About this StructureAbout this Structure
2IY5 is a Protein complex structure of sequences from Thermus thermophilus with and as ligands. Active as Phenylalanine--tRNA ligase, with EC number 6.1.1.20 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of the ternary complex of phenylalanyl-tRNA synthetase with tRNAPhe and a phenylalanyl-adenylate analogue reveals a conformational switch of the CCA end., Moor N, Kotik-Kogan O, Tworowski D, Sukhanova M, Safro M, Biochemistry. 2006 Sep 5;45(35):10572-83. PMID:16939209
Page seeded by OCA on Sun Feb 3 10:39:36 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Phenylalanine--tRNA ligase
- Protein complex
- Thermus thermophilus
- Kotik-Kogan, O.
- Moor, N.
- Safro, M.
- Sukhanova, M.
- Tworowski, D.
- FYA
- MG
- Aminoacyl-trna synthetase
- Atp-binding
- Class ii aminoacyl-trna synthetase
- Helix-turn-helix motif
- Ligase
- Magnesium
- Metal-binding
- Nucleotide-binding
- Phenylalanyl-trna synthetase
- Protein biosynthesis
- Rbd domin
- Rna-binding
- Sh3 domain
- Trna-binding