1jdi
From Proteopedia
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CRYSTAL STRUCTURE OF L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE
Overview
The structure of L-ribulose-5-phosphate 4-epimerase from E. coli has been, solved to 2.4 A resolution using X-ray diffraction data. The structure is, homo-tetrameric and displays C(4) symmetry. Each subunit has a single, domain comprised of a central beta-sheet flanked on either side by layers, of alpha-helices. The active site is identified by the position of the, catalytic zinc residue and is located at the interface between two, adjacent subunits. A remarkable feature of the structure is that it shows, a very close resemblance to that of L-fuculose-1-phosphate aldolase. This, is consistent with the notion that both enzymes belong to a superfamily of, epimerases/aldolases that catalyze carbon-carbon bond cleavage reactions, via a metal-stabilized enolate intermediate. Detailed inspection of the, epimerase structure, however, indicates that despite the close overall, structural similarity to class II aldolases, the enzyme has evolved, distinct active site features that promote its particular chemistry.
About this Structure
1JDI is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Active as L-ribulose-5-phosphate 4-epimerase, with EC number 5.1.3.4 Full crystallographic information is available from OCA.
Reference
The structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like platform for epimerization., Luo Y, Samuel J, Mosimann SC, Lee JE, Tanner ME, Strynadka NC, Biochemistry. 2001 Dec 11;40(49):14763-71. PMID:11732895
Page seeded by OCA on Tue Nov 20 18:08:19 2007
