2mbr

<table><tr><td colspan='2'>[[2mbr]] is a 1 chain structure with sequence from [http://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 [http://proteopedia.org/fgij/fg.htm?mol=2MBR FirstGlance]. <br>

</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>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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=1.3.1.98 1.3.1.98] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2mbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mbr OCA], [http://pdbe.org/2mbr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mbr RCSB], [http://www.ebi.ac.uk/pdbsum/2mbr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mbr ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MURB_ECOLI MURB_ECOLI]] Cell wall formation.

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== Publication Abstract from PubMed ==

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.

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:9020778<ref>PMID:9020778</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2mbr" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Benson, T E]]

[[Category: Hogle, J M]]

[[Category: Walsh, C T]]

[[Category: Peptidoglycan synthesis]]