9qmp

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m (Protected "9qmp" [edit=sysop:move=sysop])
Current revision (05:50, 14 May 2025) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 9qmp is ON HOLD
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==E.coli seryl-tRNA synthetase==
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<StructureSection load='9qmp' size='340' side='right'caption='[[9qmp]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9qmp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9QMP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9QMP FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.48&#8491;</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=9qmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9qmp OCA], [https://pdbe.org/9qmp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9qmp RCSB], [https://www.ebi.ac.uk/pdbsum/9qmp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9qmp ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SYS_ECOLI SYS_ECOLI] Catalyzes the attachment of serine to tRNA(Ser) (PubMed:7537870). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).<ref>PMID:2963963</ref> <ref>PMID:7537870</ref> <ref>PMID:8065908</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The three-dimensional crystal structure of seryl-transfer RNA synthetase from Escherichia coli, refined at 2.5 A resolution, is described. It has an N-terminal domain that forms an antiparallel alpha helical coiled-coil, stretching 60 A out into the solvent and stabilized by interhelical hydrophobic interactions and an active-site alpha-beta domain based around a seven-stranded antiparallel beta sheet. Unlike the three other known synthetase structures, the enzyme contains no classical nucleotide-binding fold, and is the first representative of a second class of aminoacyl-tRNA synthetase structures.
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Authors: Cusack, S.
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A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.,Cusack S, Berthet-Colominas C, Hartlein M, Nassar N, Leberman R Nature. 1990 Sep 20;347(6290):249-55. PMID:2205803<ref>PMID:2205803</ref>
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Description: E.coli seryl-tRNA synthetase
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Cusack, S]]
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<div class="pdbe-citations 9qmp" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Cusack S]]

Current revision

E.coli seryl-tRNA synthetase

PDB ID 9qmp

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