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2hsm

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==Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes==
==Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes==
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<StructureSection load='2hsm' size='340' side='right' caption='[[2hsm]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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<StructureSection load='2hsm' size='340' side='right'caption='[[2hsm]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2hsm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HSM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HSM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2hsm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HSM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HSM FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hqt|2hqt]], [[2hra|2hra]], [[2hrk|2hrk]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hqt|2hqt]], [[2hra|2hra]], [[2hrk|2hrk]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GUS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), ARC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GUS1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), ARC1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate--tRNA_ligase Glutamate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.17 6.1.1.17] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glutamate--tRNA_ligase Glutamate--tRNA ligase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.17 6.1.1.17] </span></td></tr>
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<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=2hsm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hsm OCA], [http://pdbe.org/2hsm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hsm RCSB], [http://www.ebi.ac.uk/pdbsum/2hsm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hsm ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hsm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hsm OCA], [https://pdbe.org/2hsm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hsm RCSB], [https://www.ebi.ac.uk/pdbsum/2hsm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hsm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SYEC_YEAST SYEC_YEAST]] Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (By similarity). [[http://www.uniprot.org/uniprot/G4P1_YEAST G4P1_YEAST]] Binds specifically G4 quadruplex nucleic acid structures (these are four-stranded right-handed helices, stabilized by guanine base quartets). Binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases.
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[[https://www.uniprot.org/uniprot/SYEC_YEAST SYEC_YEAST]] Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (By similarity). [[https://www.uniprot.org/uniprot/G4P1_YEAST G4P1_YEAST]] Binds specifically G4 quadruplex nucleic acid structures (these are four-stranded right-handed helices, stabilized by guanine base quartets). Binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
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*[[Aminoacyl tRNA Synthetase|Aminoacyl tRNA Synthetase]]
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Atcc 18824]]
[[Category: Atcc 18824]]
[[Category: Glutamate--tRNA ligase]]
[[Category: Glutamate--tRNA ligase]]
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[[Category: Large Structures]]
[[Category: Simader, H]]
[[Category: Simader, H]]
[[Category: Suck, D]]
[[Category: Suck, D]]
[[Category: Ligase-rna binding protein complex]]
[[Category: Ligase-rna binding protein complex]]
[[Category: Protein complex protein interaction gst-fold]]
[[Category: Protein complex protein interaction gst-fold]]

Revision as of 07:21, 24 March 2021

Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes

PDB ID 2hsm

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