2ixh: Difference between revisions
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Revision as of 18:14, 30 October 2007
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RMLC P AERUGINOSA WITH DTDP-RHAMNOSE
OverviewOverview
The striking feature of carbohydrates is their constitutional, conformational and configurational diversity. Biology has harnessed this, diversity and manipulates carbohydrate residues in a variety of ways, one, of which is epimerization. RmlC catalyzes the epimerization of the C3' and, C5' positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming, dTDP-6-deoxy-L-lyxo-4-hexulose. RmlC is the third enzyme of the rhamnose, pathway, and represents a validated anti-bacterial drug target. Although, several structures of the enzyme have been reported, the mechanism and the, nature of the intermediates have remained obscure. Despite its relatively, small size (22 kDa), RmlC catalyzes four stereospecific proton transfers, and the substrate undergoes a major conformational change during the, course of ... [(full description)]
About this StructureAbout this Structure
2IXH is a [Single protein] structure of sequence from [Pseudomonas aeruginosa] with TRH as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
RmlC, a C3' and C5' carbohydrate epimerase, appears to operate via an intermediate with an unusual twist boat conformation., Dong C, Major LL, Srikannathasan V, Errey JC, Giraud MF, Lam JS, Graninger M, Messner P, McNeil MR, Field RA, Whitfield C, Naismith JH, J Mol Biol. 2007 Jan 5;365(1):146-59. Epub 2006 Sep 29. PMID:17046787
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