1mbb

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(New page: 200px<br /><applet load="1mbb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mbb, resolution 2.30&Aring;" /> '''OXIDOREDUCTASE'''<br...)
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[[Image:1mbb.gif|left|200px]]<br /><applet load="1mbb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mbb, resolution 2.30&Aring;" />
 
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'''OXIDOREDUCTASE'''<br />
 
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==Overview==
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==OXIDOREDUCTASE==
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UDP-N-acetylenolpyruvylglucosamine reductase (MurB), a peptidoglycan, biosynthetic enzyme from Escherichia coli, reduces both (E)- and, (Z)-isomers of enolbutyryl-UDP-GlcNAc, C4 analogs of the physiological C3, enolpyruvyl substrate, to UDP-methyl-N-acetylmuramic acid in the presence, of NADPH. The X-ray crystal structure of the, (E)-enolbutyryl-UDP-GlcNAc-MurB complex is similar to that of the, enolpyruvyl-UDP-GlcNAc-MurB complex. In both structures the groups thought, to be involved in hydride transfer to C3 and protonation at C2 of the enol, ether substrate are arranged anti relative to the enol double bond. The, stereochemical outcome of reduction of (E)-enolbutyryl-UDP-GlcNAc by NADPD, in D2O is thus predicted to yield a (2R,3R)-dideuterio product. This was, validated by conversion of the 2,3-dideuterio-UDP-methyl-N-acetylmuramic, acid product to 2,3-dideuterio-2-hydroxybutyrate, which was shown to be, (2R) by enzymatic analysis and (3R) by NMR comparison to authentic, (2R,3R)- and (2R,3S)-2,3-dideuterio-2-hydroxybutyrate. Remarkably, the, (E)-enolbutyryl-UDP-GlcNAc was found to partition between reduction to, UDP-methyl-N-acetylmuramic and isomerization to the (Z)-substrate isomer, in the MurB active site, indicative of a C2 carbanion/enol species that is, sufficiently long-lived to rotate around the C2-C3 single bond during, catalysis.
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<StructureSection load='1mbb' size='340' side='right'caption='[[1mbb]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1mbb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MBB FirstGlance]. <br>
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1MBB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with EEB and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/UDP-N-acetylmuramate_dehydrogenase UDP-N-acetylmuramate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.158 1.1.1.158] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MBB 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]] 2.3&#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=EEB:URIDINE-DIPHOSPHATE-3(N-ACETYLGLUCOSAMINYL)BUTYRIC+ACID'>EEB</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=1mbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mbb OCA], [https://pdbe.org/1mbb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mbb RCSB], [https://www.ebi.ac.uk/pdbsum/1mbb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mbb ProSAT]</span></td></tr>
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(E)-enolbutyryl-UDP-N-acetylglucosamine as a mechanistic probe of UDP-N-acetylenolpyruvylglucosamine reductase (MurB)., Lees WJ, Benson TE, Hogle JM, Walsh CT, Biochemistry. 1996 Feb 6;35(5):1342-51. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8634262 8634262]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MURB_ECOLI MURB_ECOLI] Cell wall formation.
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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/mb/1mbb_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=1mbb ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: UDP-N-acetylmuramate dehydrogenase]]
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[[Category: Benson TE]]
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[[Category: Benson, T.E.]]
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[[Category: Hogle JM]]
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[[Category: Hogle, J.M.]]
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[[Category: Lees WJ]]
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[[Category: Lees, W.J.]]
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[[Category: Walsh CT]]
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[[Category: Walsh, C.T.]]
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[[Category: EEB]]
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[[Category: FAD]]
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[[Category: flavoenzyme]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:17:47 2007''
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Current revision

OXIDOREDUCTASE

PDB ID 1mbb

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