3foc: Difference between revisions

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==Tryptophanyl-tRNA synthetase from Giardia lamblia==
==Tryptophanyl-tRNA synthetase from Giardia lamblia==
<StructureSection load='3foc' size='340' side='right' caption='[[3foc]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
<StructureSection load='3foc' size='340' side='right'caption='[[3foc]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3foc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Giaic Giaic]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FOC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FOC FirstGlance]. <br>
<table><tr><td colspan='2'>[[3foc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Giaic Giaic]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FOC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FOC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GL50803_3032 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=184922 GIAIC])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GL50803_3032 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=184922 GIAIC])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan--tRNA_ligase Tryptophan--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.2 6.1.1.2] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tryptophan--tRNA_ligase Tryptophan--tRNA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.2 6.1.1.2] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3foc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3foc OCA], [http://pdbe.org/3foc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3foc RCSB], [http://www.ebi.ac.uk/pdbsum/3foc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3foc ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3foc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3foc OCA], [https://pdbe.org/3foc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3foc RCSB], [https://www.ebi.ac.uk/pdbsum/3foc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3foc ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/3foc_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/3foc_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</div>
</div>
<div class="pdbe-citations 3foc" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3foc" style="background-color:#fffaf0;"></div>
==See Also==
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Giaic]]
[[Category: Giaic]]
[[Category: Large Structures]]
[[Category: Tryptophan--tRNA ligase]]
[[Category: Tryptophan--tRNA ligase]]
[[Category: Arakaki, T L]]
[[Category: Arakaki, T L]]

Revision as of 11:06, 2 March 2022

Tryptophanyl-tRNA synthetase from Giardia lambliaTryptophanyl-tRNA synthetase from Giardia lamblia

Structural highlights

3foc is a 2 chain structure with sequence from Giaic. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:GL50803_3032 (GIAIC)
Activity:Tryptophan--tRNA ligase, with EC number 6.1.1.2
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The 2.1A crystal structure of tryptophanyl-tRNA synthetase (TrpRS) from the diplomonad Giardia lamblia reveals that the N-terminus of this class I aminoacyl-tRNA synthetase forms a 16-residue alpha-helix. This helix replaces a beta-hairpin that is required by human TrpRS for normal activity and has been inferred to play a similar role in all eukaryotic TrpRS. The primary sequences of TrpRS homologs from several basal eukaryotes including Giardia lack a set of three residues observed to stabilize interactions with this beta-hairpin in the human TrpRS. Thus the present structure suggests that the activation reaction mechanism of TrpRS from the basal eukaryote G. lamblia differs from that of higher eukaryotes. Furthermore, the protein as observed in the crystal forms an (alpha(2))(2) homotetramer. The canonical dimer interface observed in all previous structures of tryptophanyl-tRNA synthetases is maintained, but in addition each N-terminal alpha-helix reciprocally interlocks with the equivalent helix from a second dimer to form a dimer of dimers. Although we have no evidence for tetramer formation in vivo, modeling indicates that the crystallographically observed tetrameric structure would be compatible with the tRNA binding mode used by dimeric TrpRS and TyrRS.

The structure of tryptophanyl-tRNA synthetase from Giardia lamblia reveals divergence from eukaryotic homologs.,Arakaki TL, Carter M, Napuli AJ, Verlinde CL, Fan E, Zucker F, Buckner FS, Van Voorhis WC, Hol WG, Merritt EA J Struct Biol. 2010 Aug;171(2):238-43. Epub 2010 May 8. PMID:20438846[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Arakaki TL, Carter M, Napuli AJ, Verlinde CL, Fan E, Zucker F, Buckner FS, Van Voorhis WC, Hol WG, Merritt EA. The structure of tryptophanyl-tRNA synthetase from Giardia lamblia reveals divergence from eukaryotic homologs. J Struct Biol. 2010 Aug;171(2):238-43. Epub 2010 May 8. PMID:20438846 doi:10.1016/j.jsb.2010.04.010

3foc, resolution 2.09Å

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