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[[Image:2mbr.jpg|left|200px]]<br /><applet load="2mbr" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2mbr, resolution 1.80&Aring;" />
'''MURB WILD TYPE, COMPLEX WITH ENOLPYRUVYL-UDP-N-ACETYLGLUCOSAMINE'''<br />


==Overview==
==MURB WILD TYPE, COMPLEX WITH ENOLPYRUVYL-UDP-N-ACETYLGLUCOSAMINE==
MurB catalyzes the second committed step in the synthesis of peptidoglycan, a key component of the bacterial cell wall. The crystal structures of both a S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine were solved and refined at 1.8 A resolution. The single point mutation of residue 229 from serine to alanine eliminated a hydroxyl group which has previously been proposed to play a critical role as a proton donor during the second half-reaction of MurB, namely, reoxidation of FADH2 and reduction of the enolpyruvyl substrate. The mutation also resulted in the loss of the water molecule-hydrogen bonded to the serine hydroxyl in the wild-type structure changing the hydrogen-bonding network with in the active site. Comparison of the wild-type and S229A mutant structures confirms that the dramatic kinetic defect of an approximately 10(7)-fold decrease observed for the Ser 229 Ala mutant in the second half-reaction [Benson, T.E., Walsh, C.T., &amp; Massey, V. (1997) Biochemistry 36, 796-805] is a direct result of the loss of the serine hydroxyl moiety rather than other nonspecific active-site changes or general structural defects.
<StructureSection load='2mbr' size='340' side='right'caption='[[2mbr]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[2mbr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mbr 1mbr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MBR FirstGlance]. <br>
2MBR 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 <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=EPU:'>EPU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1MBR. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBR OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPU:URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL)+BUTYRIC+ACID'>EPU</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mbr OCA], [https://pdbe.org/2mbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mbr RCSB], [https://www.ebi.ac.uk/pdbsum/2mbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mbr ProSAT]</span></td></tr>
X-ray crystal structures of the S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine at 1.8-A resolution., Benson TE, Walsh CT, Hogle JM, Biochemistry. 1997 Jan 28;36(4):806-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9020778 9020778]
</table>
== Function ==
[https://www.uniprot.org/uniprot/MURB_ECOLI MURB_ECOLI] Cell wall formation.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mb/2mbr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2mbr ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[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: Walsh CT]]
[[Category: Walsh, C T.]]
[[Category: EPU]]
[[Category: FAD]]
[[Category: cell division]]
[[Category: cell wall]]
[[Category: fad]]
[[Category: flavoprotein]]
[[Category: nadp]]
[[Category: oxidoreductase]]
[[Category: peptidoglycan synthesis]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:27 2008''

Latest revision as of 09:05, 21 February 2024

MURB WILD TYPE, COMPLEX WITH ENOLPYRUVYL-UDP-N-ACETYLGLUCOSAMINE

2mbr, resolution 1.80Å

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