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1mbb

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OXIDOREDUCTASE

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Retrieved from "http://52.214.119.220/wiki/index.php/1mbb"

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-[[Image:1mbb.gif|left|200px]]
- {{Structure
+==OXIDOREDUCTASE==
-|PDB= 1mbb |SIZE=350|CAPTION= <scene name='initialview01'>1mbb</scene>, resolution 2.30&Aring;
+<StructureSection load='1mbb' size='340' side='right'caption='[[1mbb]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=EEB:URIDINE-DIPHOSPHATE-3(N-ACETYLGLUCOSAMINYL)BUTYRIC+ACID'>EEB</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
+<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>
-|ACTIVITY= [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]
+</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>
-|GENE=
+<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>
-}}
+<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>
+</table>
-'''OXIDOREDUCTASE'''
+== Function ==
+[https://www.uniprot.org/uniprot/MURB_ECOLI MURB_ECOLI] Cell wall formation.
+== Evolutionary Conservation ==
-==Overview==
+[[Image:Consurf_key_small.gif|200px|right]]
-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.
+Check<jmol>
+  <jmolCheckbox>
-==About this Structure==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mb/1mbb_consurf.spt"</scriptWhenChecked>
-MBB is a [[Single protein]] structure of sequence from [http://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].
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==Reference==
+  </jmolCheckbox>
-(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://www.ncbi.nlm.nih.gov/pubmed/8634262 8634262]
+</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].
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: UDP-N-acetylmuramate dehydrogenase]]
+[[Category: Benson TE]]
-[[Category: Benson, T E.]]
+[[Category: Hogle JM]]
-[[Category: Hogle, J M.]]
+[[Category: Lees WJ]]
-[[Category: Lees, W J.]]
+[[Category: Walsh CT]]
-[[Category: Walsh, C T.]]
-[[Category: EEB]]
-[[Category: FAD]]
-[[Category: flavoenzyme]]
-[[Category: oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:41:21 2008''

1mbb

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OXIDOREDUCTASE

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