2hk2

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(New page: 200px<br /><applet load="2hk2" size="350" color="white" frame="true" align="right" spinBox="true" caption="2hk2, resolution 2.300&Aring;" /> '''Crystal structure o...)
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[[Image:2hk2.jpg|left|200px]]<br /><applet load="2hk2" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2hk2, resolution 2.300&Aring;" />
 
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'''Crystal structure of mevalonate diphosphate decarboxylase from Staphylococcus aureus (monoclinic form)'''<br />
 
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==Overview==
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==Crystal structure of mevalonate diphosphate decarboxylase from Staphylococcus aureus (monoclinic form)==
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Mevalonate diphosphate decarboxylase (MDD) catalyzes the ATP-dependent, decarboxylation of mevalonate 5-diphosphate (MDP) to form isopentenyl, pyrophosphate, a ubiquitous precursor for isoprenoid biosynthesis. MDD is, a poorly understood component of this important metabolic pathway., Complementation of a temperature-sensitive yeast mutant by the putative, mdd genes of Trypanosoma brucei and Staphylococcus aureus provides, proof-of-function. Crystal structures of MDD from T. brucei (TbMDD, at 1.8, A resolution) and S. aureus (SaMDD, in two distinct crystal forms, each, diffracting to 2.3 A resolution) have been determined. Gel-filtration, chromatography and analytical ultracentrifugation experiments indicate, that TbMDD is predominantly monomeric in solution while SaMDD is dimeric., The new crystal structures and comparison with that of the yeast, Saccharomyces cerevisiae enzyme (ScMDD) reveal the structural basis for, this variance in quaternary structure. The presence of an ordered sulfate, in the structure of TbMDD reveals for the first time details of a ligand, binding in the MDD active site and, in conjunction with well-ordered water, molecules, comparisons with the related enzyme mevalonate kinase, structural and biochemical data derived on ScMDD and SaMDD, allows us to, model a ternary complex with MDP and ATP. This model facilitates, discussion of the molecular determinants of substrate recognition and, contributions made by specific residues to the enzyme mechanism.
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<StructureSection load='2hk2' size='340' side='right'caption='[[2hk2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2hk2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HK2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HK2 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]] 2.3&#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=2hk2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hk2 OCA], [https://pdbe.org/2hk2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hk2 RCSB], [https://www.ebi.ac.uk/pdbsum/2hk2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hk2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9FD84_STAAU Q9FD84_STAAU]
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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/hk/2hk2_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=2hk2 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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2HK2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Active as [http://en.wikipedia.org/wiki/Diphosphomevalonate_decarboxylase Diphosphomevalonate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.33 4.1.1.33] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HK2 OCA].
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*[[Albumin 3D structures|Albumin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal Structures of Trypanosoma brucei and Staphylococcus aureus Mevalonate Diphosphate Decarboxylase Inform on the Determinants of Specificity and Reactivity., Byres E, Alphey MS, Smith TK, Hunter WN, J Mol Biol. 2007 Aug 10;371(2):540-53. Epub 2007 Jun 4. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17583736 17583736]
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[[Category: Large Structures]]
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[[Category: Diphosphomevalonate decarboxylase]]
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[[Category: Single protein]]
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[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
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[[Category: Byres, E.]]
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[[Category: Byres E]]
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[[Category: Hunter, W.N.]]
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[[Category: Hunter WN]]
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[[Category: decarboxylase]]
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[[Category: diphosphomevalonate decarboxylase]]
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[[Category: mevalonate diphosphate decarboxylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:14:07 2008''
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Current revision

Crystal structure of mevalonate diphosphate decarboxylase from Staphylococcus aureus (monoclinic form)

PDB ID 2hk2

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