1oy0

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(New page: 200px<br /><applet load="1oy0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oy0, resolution 2.80&Aring;" /> '''The crystal Structur...)
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[[Image:1oy0.gif|left|200px]]<br /><applet load="1oy0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1oy0, resolution 2.80&Aring;" />
 
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'''The crystal Structure of the First Enzyme of Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase from Mycobacterium Tuberculosis Shows a Decameric Assembly and Terminal Helix-Swapping'''<br />
 
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==Overview==
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==The crystal Structure of the First Enzyme of Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase from Mycobacterium Tuberculosis Shows a Decameric Assembly and Terminal Helix-Swapping==
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Ketopantoate hydroxymethyltransferase (KPHMT) catalyzes the first, committed step in the biosynthesis of pantothenate, which is a precursor, to coenzyme A and is required for penicillin biosynthesis. The crystal, structure of KPHMT from Mycobacterium tuberculosis was determined by the, single anomalous substitution (SAS) method at 2.8 A resolution. KPHMT, adopts a structure that is a variation on the (beta/alpha) barrel fold, with a metal binding site proximal to the presumed catalytic site. The, protein forms a decameric complex, with subunits in opposing pentameric, rings held together by a swapping of their C-terminal alpha helices. The, structure reveals KPHMT's membership in a small, recently discovered group, of (beta/alpha) barrel enzymes that employ domain swapping to form a, variety of oligomeric assemblies. The apparent conservation of certain, detailed structural characteristics suggests that KPHMT is distantly, related by divergent evolution to enzymes in unrelated pathways, including, isocitrate lyase and phosphoenolpyruvate mutase.
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<StructureSection load='1oy0' size='340' side='right'caption='[[1oy0]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1oy0]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OY0 FirstGlance]. <br>
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1OY0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/3-methyl-2-oxobutanoate_hydroxymethyltransferase 3-methyl-2-oxobutanoate hydroxymethyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.11 2.1.2.11] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OY0 OCA].
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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]] 2.8&#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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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==Reference==
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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=1oy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oy0 OCA], [https://pdbe.org/1oy0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oy0 RCSB], [https://www.ebi.ac.uk/pdbsum/1oy0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oy0 ProSAT]</span></td></tr>
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The crystal structure of the first enzyme in the pantothenate biosynthetic pathway, ketopantoate hydroxymethyltransferase, from M tuberculosis., Chaudhuri BN, Sawaya MR, Kim CY, Waldo GS, Park MS, Terwilliger TC, Yeates TO, Structure. 2003 Jul;11(7):753-64. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12842039 12842039]
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</table>
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[[Category: 3-methyl-2-oxobutanoate hydroxymethyltransferase]]
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== Function ==
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[https://www.uniprot.org/uniprot/PANB_MYCTU PANB_MYCTU] Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is tranferred onto alpha-ketoisovalerate to form ketopantoate.<ref>PMID:12515554</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/oy/1oy0_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=1oy0 ConSurf].
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<div style="clear:both"></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: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
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[[Category: Single protein]]
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[[Category: Chaudhuri BN]]
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[[Category: Chaudhuri, B.N.]]
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[[Category: Kim CY]]
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[[Category: Kim, C.Y.]]
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[[Category: Park MS]]
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[[Category: Park, M.S.]]
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[[Category: Sawaya MR]]
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[[Category: Sawaya, M.R.]]
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[[Category: Terwilliger TC]]
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[[Category: TBSGC, TB.Structural.Genomics.Consortium.]]
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[[Category: Waldo GS]]
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[[Category: Terwilliger, T.C.]]
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[[Category: Yeates TO]]
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[[Category: Waldo, G.S.]]
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[[Category: Yeates, T.O.]]
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[[Category: MG]]
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[[Category: domain swapping]]
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[[Category: protein structure initiative]]
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[[Category: psi]]
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[[Category: structural genomics]]
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[[Category: tb structural genomics consortium]]
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[[Category: tbsgc]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:17:10 2007''
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Current revision

The crystal Structure of the First Enzyme of Pantothenate Biosynthetic Pathway, Ketopantoate Hydroxymethyltransferase from Mycobacterium Tuberculosis Shows a Decameric Assembly and Terminal Helix-Swapping

PDB ID 1oy0

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