1mbt

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(New page: 200px<br /><applet load="1mbt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mbt, resolution 3.0&Aring;" /> '''OXIDOREDUCTASE'''<br ...)
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[[Image:1mbt.jpg|left|200px]]<br /><applet load="1mbt" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mbt, resolution 3.0&Aring;" />
 
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'''OXIDOREDUCTASE'''<br />
 
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==Overview==
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==OXIDOREDUCTASE==
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BACKGROUND: The repeating disaccharide and pentapeptide units of the, bacterial peptidoglycan layer are connected by a lactyl ether bridge, biosynthesized from UDP-N-acetylglucosamine and phosphoenolpyruvate in, sequential enol ether transfer and reduction steps catalyzed by MurA and, MurB respectively. Knowledge of the structure and mechanism of the MurB, enzyme will permit analysis of this unusual enol ether reduction reaction, and may facilitate the design of inhibitors as candidate next-generation, antimicrobial agents. RESULTS: The crystal structure of, UDP-N-acetylenolpyruvylglucosamine reductase, MurB, has been solved at 3.0, A and compared with our previously reported structure of MurB complexed, with its substrate enolpyruvyl-UDP-N- acetylglucosamine. Comparison of the, liganded structure of MurB with this unliganded form reveals that the, binding of substrate induces a substantial movement of domain 3 (residues, 219-319) of the enzyme and a significant rearrangement of a loop within, this domain. These ligand induced changes disrupt a stacking interaction, between two tyrosines (Tyr190 and Tyr254) which lie at the side of the, channel leading to the active site of the free enzyme. CONCLUSIONS: The, conformational change induced by enolpyruvyl-UDP-N- acetylglucosamine, binding to MurB results in the closure of the substrate-binding channel, over the substrate. Tyr190 swings over the channel opening and establishes, a hydrogen bond with an oxygen of the alpha-phosphate of the sugar, nucleotide substrate which is critical to substrate binding.
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<StructureSection load='1mbt' size='340' side='right'caption='[[1mbt]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1mbt]] 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=1MBT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MBT FirstGlance]. <br>
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1MBT 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 SO4 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=1MBT 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]] 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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1mbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mbt OCA], [https://pdbe.org/1mbt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mbt RCSB], [https://www.ebi.ac.uk/pdbsum/1mbt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mbt ProSAT]</span></td></tr>
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The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls., Benson TE, Walsh CT, Hogle JM, Structure. 1996 Jan 15;4(1):47-54. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8805513 8805513]
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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/1mbt_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=1mbt 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: Walsh CT]]
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[[Category: Walsh, C.T.]]
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[[Category: FAD]]
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[[Category: SO4]]
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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 21:18:53 2007''
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Current revision

OXIDOREDUCTASE

PDB ID 1mbt

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