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| | ==THE CRYSTAL STRUCTURE OF UMP KINASE FROM BACILLUS ANTHRACIS (BA1797)== | | ==THE CRYSTAL STRUCTURE OF UMP KINASE FROM BACILLUS ANTHRACIS (BA1797)== |
| - | <StructureSection load='2jjx' size='340' side='right' caption='[[2jjx]], [[Resolution|resolution]] 2.82Å' scene=''> | + | <StructureSection load='2jjx' size='340' side='right'caption='[[2jjx]], [[Resolution|resolution]] 2.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jjx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis_(strain_ames) Bacillus anthracis (strain 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JJX FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.82Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UMP_kinase UMP kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.22 2.7.4.22] </span></td></tr> | + | <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> |
| - | <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=2jjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jjx OCA], [http://pdbe.org/2jjx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jjx RCSB], [http://www.ebi.ac.uk/pdbsum/2jjx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jjx 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=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> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A6L7HKK4_BACAN A0A6L7HKK4_BACAN] Catalyzes the reversible phosphorylation of UMP to UDP.[HAMAP-Rule:MF_01220] |
| | == 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: UMP kinase]] | + | [[Category: Bacillus anthracis str. Ames]] |
| - | [[Category: Carter, L G]] | + | [[Category: Large Structures]] |
| - | [[Category: Esnouf, R M]] | + | [[Category: Carter LG]] |
| - | [[Category: Mancini, E J]] | + | [[Category: Esnouf RM]] |
| - | [[Category: Meier, C]] | + | [[Category: Mancini EJ]] |
| - | [[Category: OPPF, Oxford Protein Production Facility]] | + | [[Category: Meier C]] |
| - | [[Category: Owens, R J]] | + | [[Category: Owens RJ]] |
| - | [[Category: SPINE, Structural Proteomics in Europe]]
| + | [[Category: Stuart DI]] |
| - | [[Category: Stuart, D I]] | + | |
| - | [[Category: Atp-binding]]
| + | |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Oppf]]
| + | |
| - | [[Category: Pyrh]]
| + | |
| - | [[Category: Pyrimidine biosynthesis]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Uridylate kinase]]
| + | |
| Structural highlights
Function
A0A6L7HKK4_BACAN Catalyzes the reversible phosphorylation of UMP to UDP.[HAMAP-Rule:MF_01220]
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
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Meier C, Carter LG, Sainsbury S, Mancini EJ, Owens RJ, Stuart DI, Esnouf RM. The crystal structure of UMP kinase from Bacillus anthracis (BA1797) reveals an allosteric nucleotide-binding site. J Mol Biol. 2008 Sep 19;381(5):1098-105. Epub 2008 Jul 3. PMID:18625239 doi:10.1016/j.jmb.2008.06.078
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