2hz7: Difference between revisions
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<StructureSection load='2hz7' size='340' side='right'caption='[[2hz7]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2hz7' size='340' side='right'caption='[[2hz7]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2hz7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2hz7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HZ7 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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=2hz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hz7 OCA], [https://pdbe.org/2hz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hz7 RCSB], [https://www.ebi.ac.uk/pdbsum/2hz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hz7 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=2hz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hz7 OCA], [https://pdbe.org/2hz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hz7 RCSB], [https://www.ebi.ac.uk/pdbsum/2hz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hz7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/SYQ_DEIRA SYQ_DEIRA] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Deinococcus radiodurans]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Becker | [[Category: Becker HD]] | ||
[[Category: Deniziak | [[Category: Deniziak M]] | ||
[[Category: Giege | [[Category: Giege R]] | ||
[[Category: Kern | [[Category: Kern D]] | ||
[[Category: Paulus | [[Category: Paulus C]] | ||
[[Category: Sauter | [[Category: Sauter C]] | ||
Latest revision as of 13:03, 30 August 2023
Crystal structure of the Glutaminyl-tRNA synthetase from Deinococcus radioduransCrystal structure of the Glutaminyl-tRNA synthetase from Deinococcus radiodurans
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGlutaminyl-tRNA synthetase from Deinococcus radiodurans possesses a C-terminal extension of 215 residues appending the anticodon-binding domain. This domain constitutes a paralog of the Yqey protein present in various organisms and part of it is present in the C-terminal end of the GatB subunit of GatCAB, a partner of the indirect pathway of Gln-tRNA(Gln) formation. To analyze the peculiarities of the structure-function relationship of this GlnRS related to the Yqey domain, a structure of the protein was solved from crystals diffracting at 2.3 A and a docking model of the synthetase complexed to tRNA(Gln) constructed. The comparison of the modeled complex with the structure of the E. coli complex reveals that all residues of E. coli GlnRS contacting tRNA(Gln) are conserved in D. radiodurans GlnRS, leaving the functional role of the Yqey domain puzzling. Kinetic investigations and tRNA-binding experiments of full length and Yqey-truncated GlnRSs reveal that the Yqey domain is involved in tRNA(Gln) recognition. They demonstrate that Yqey plays the role of an affinity-enhancer of GlnRS for tRNA(Gln) acting only in cis. However, the presence of Yqey in free state in organisms lacking GlnRS, suggests that this domain may exert additional cellular functions. Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation.,Deniziak M, Sauter C, Becker HD, Paulus CA, Giege R, Kern D Nucleic Acids Res. 2007;35(5):1421-31. Epub 2007 Feb 6. PMID:17284460[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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