2bmu

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(New page: 200px<br /> <applet load="2bmu" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bmu, resolution 2.55&Aring;" /> '''UMP KINASE FROM PYR...)
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[[Image:2bmu.gif|left|200px]]<br />
 
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<applet load="2bmu" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2bmu, resolution 2.55&Aring;" />
 
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'''UMP KINASE FROM PYROCOCCUS FURIOSUS COMPLEXED WITH ITS SUBSTRATE UMP AND ITS SUBSTRATE ANALOG AMPPNP'''<br />
 
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==Overview==
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==UMP KINASE FROM PYROCOCCUS FURIOSUS COMPLEXED WITH ITS SUBSTRATE UMP AND ITS SUBSTRATE ANALOG AMPPNP==
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UMP kinase (UMPK), the enzyme responsible for microbial UMP, phosphorylation, plays a key role in pyrimidine nucleotide biosynthesis, regulating this process via feed-back control and via gene repression of, carbamoyl phosphate synthetase (the first enzyme of the pyrimidine, biosynthesis pathway). We present crystal structures of Pyrococcus, furiosus UMPK, free or complexed with AMPPNP or AMPPNP and UMP, at 2.4 A, 3 A and 2.55 A resolution, respectively, providing a true snapshot of the, catalytically competent bisubstrate complex. The structure proves that, UMPK does not resemble other nucleoside monophosphate kinases, including, the UMP/CMP kinase found in animals, and thus UMPK may be a potential, antimicrobial target. This enzyme has a homohexameric architecture centred, around a ... [[http://ispc.weizmann.ac.il/pmbin/getpm?16095620 (full description)]]
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<StructureSection load='2bmu' size='340' side='right'caption='[[2bmu]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2bmu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BMU 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]] 2.55&#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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</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=2bmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bmu OCA], [https://pdbe.org/2bmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bmu RCSB], [https://www.ebi.ac.uk/pdbsum/2bmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bmu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PYRH_PYRFU PYRH_PYRFU] Catalyzes the reversible phosphorylation of UMP to UDP, with ATP as the most efficient phosphate donor.<ref>PMID:15698963</ref>
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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/bm/2bmu_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=2bmu ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2BMU is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]] with MG, ANP and U5P as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BMU OCA]].
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*[[Uridylate kinase|Uridylate kinase]]
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== References ==
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==Reference==
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<references/>
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The crystal structure of Pyrococcus furiosus UMP kinase provides insight into catalysis and regulation in microbial pyrimidine nucleotide biosynthesis., Marco-Marin C, Gil-Ortiz F, Rubio V, J Mol Biol. 2005 Sep 16;352(2):438-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16095620 16095620]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
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[[Category: Single protein]]
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[[Category: Gil-Ortiz F]]
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[[Category: Gil-Ortiz, F.]]
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[[Category: Marco-Marin C]]
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[[Category: Marco-Marin, C.]]
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[[Category: Rubio V]]
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[[Category: Rubio, V.]]
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[[Category: ANP]]
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[[Category: MG]]
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[[Category: U5P]]
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[[Category: amino acid kinase]]
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[[Category: phosphoryl group transfer]]
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[[Category: pyrimidine biosynthesis]]
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[[Category: transferase]]
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[[Category: ump kinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:48:48 2007''
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Current revision

UMP KINASE FROM PYROCOCCUS FURIOSUS COMPLEXED WITH ITS SUBSTRATE UMP AND ITS SUBSTRATE ANALOG AMPPNP

PDB ID 2bmu

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