1x92

<table><tr><td colspan='2'>[[1x92]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X92 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1X92 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M7P:D-GLYCERO-D-MANNOPYRANOSE-7-PHOSPHATE'>M7P</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpcA, gmhA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=1x92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x92 OCA], [http://pdbe.org/1x92 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1x92 RCSB], [http://www.ebi.ac.uk/pdbsum/1x92 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1x92 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/GMHA_PSEAE GMHA_PSEAE]] Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate (By similarity).

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== Publication Abstract from PubMed ==

The barrier imposed by lipopolysaccharide (LPS) in the outer membrane of Gram-negative bacteria presents a significant challenge in treatment of these organisms with otherwise effective hydrophobic antibiotics. The absence of L-glycero-D-manno-heptose in the LPS molecule is associated with a dramatically increased bacterial susceptibility to hydrophobic antibiotics and thus enzymes in the ADP-heptose biosynthesis pathway are of significant interest. GmhA catalyzes the isomerization of D-sedoheptulose 7-phosphate into D-glycero-D-manno-heptose 7-phosphate, the first committed step in the formation of ADP-heptose. Here we report structures of GmhA from Escherichia coli and Pseudomonas aeruginosa in apo, substrate, and product-bound forms, which together suggest that GmhA adopts two distinct conformations during isomerization through reorganization of quaternary structure. Biochemical characterization of GmhA mutants, combined with in vivo analysis of LPS biosynthesis and novobiocin susceptibility, identifies key catalytic residues. We postulate GmhA acts through an enediol-intermediate isomerase mechanism.

Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antibiotic adjuvants.,Taylor PL, Blakely KM, de Leon GP, Walker JR, McArthur F, Evdokimova E, Zhang K, Valvano MA, Wright GD, Junop MS J Biol Chem. 2008 Feb 1;283(5):2835-45. Epub 2007 Dec 3. PMID:18056714<ref>PMID:18056714</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 1x92" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Edwards, A]]

[[Category: Evdokimova, E]]

[[Category: Joachimiak, A]]

[[Category: Kudritska, M]]

[[Category: Structural genomic]]

[[Category: Savchenko, A]]

[[Category: Walker, J R]]

[[Category: Sis domain]]