2jjx

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(New page: '''Unreleased structure''' The entry 2jjx is ON HOLD Authors: MEIER, C., CARTER, L.G., MANCINI, E.J., OWENS, R.J., STUART, D.I., ESNOUF, R.M., OXFORD PROTEIN PRODUCTION FACILITY (OPPF),...)
Current revision (14:52, 13 December 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 2jjx is ON HOLD
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==THE CRYSTAL STRUCTURE OF UMP KINASE FROM BACILLUS ANTHRACIS (BA1797)==
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<StructureSection load='2jjx' size='340' side='right'caption='[[2jjx]], [[Resolution|resolution]] 2.82&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2jjx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_str._Ames Bacillus anthracis str. Ames]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JJX 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]] 2.82&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2jjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jjx OCA], [https://pdbe.org/2jjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jjx RCSB], [https://www.ebi.ac.uk/pdbsum/2jjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jjx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A6L7HKK4_BACAN A0A6L7HKK4_BACAN] Catalyzes the reversible phosphorylation of UMP to UDP.[HAMAP-Rule:MF_01220]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jj/2jjx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jjx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Uridine monophosphate (UMP) kinase is a conserved enzyme that catalyzes the ATP-driven conversion of uridylate monophosphate into uridylate diphosphate, an essential metabolic step. In prokaryotes, the enzyme exists as a homohexamer that is regulated by various metabolites. Whereas the enzymatic mechanism of UMP kinase (UK) is well-characterized, the molecular basis of its regulation remains poorly understood. Here we report the crystal structure of UK from Bacillus anthracis (BA1797) in complex with ATP at 2.82 A resolution. It reveals that the cofactor, in addition to binding in the active sites, also interacts with separate binding pockets located near the center of the hexameric structure. The existence of such an allosteric binding site had been predicted by biochemical studies, but it was not identified in previous crystal structures of prokaryotic UKs. We show that this putative allosteric pocket is conserved across different bacterial species, suggesting that it is a feature common to bacterial UKs, and we present a structural model for the allosteric regulation of this enzyme.
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Authors: MEIER, C., CARTER, L.G., MANCINI, E.J., OWENS, R.J., STUART, D.I., ESNOUF, R.M., OXFORD PROTEIN PRODUCTION FACILITY (OPPF), STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
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The crystal structure of UMP kinase from Bacillus anthracis (BA1797) reveals an allosteric nucleotide-binding site.,Meier C, Carter LG, Sainsbury S, Mancini EJ, Owens RJ, Stuart DI, Esnouf RM J Mol Biol. 2008 Sep 19;381(5):1098-105. Epub 2008 Jul 3. PMID:18625239<ref>PMID:18625239</ref>
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Description: THE CRYSTAL STRUCTURE OF UMP KINASE FROM BACILLUS ANTHRACIS (BA1797)
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 11 08:31:44 2008''
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</div>
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<div class="pdbe-citations 2jjx" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Uridylate kinase|Uridylate kinase]]
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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: Bacillus anthracis str. Ames]]
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[[Category: Large Structures]]
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[[Category: Carter LG]]
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[[Category: Esnouf RM]]
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[[Category: Mancini EJ]]
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[[Category: Meier C]]
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[[Category: Owens RJ]]
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[[Category: Stuart DI]]

Current revision

THE CRYSTAL STRUCTURE OF UMP KINASE FROM BACILLUS ANTHRACIS (BA1797)

PDB ID 2jjx

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