1w57
From Proteopedia
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STRUCTURE OF THE BIFUNCTIONAL ISPDF FROM CAMPYLOBACTER JEJUNI CONTAINING ZN
Overview
The bifunctional methylerythritol 4-phosphate cytidylyltransferase, methylerythritol 2,4-cyclodiphosphate synthase (IspDF) is unusual in that, it catalyzes nonconsecutive reactions in the 1-deoxy-D-xylulose, 5-phosphate (DOXP) pathway of isoprenoid precursor biosynthesis. The, crystal structure of IspDF from the bacterial pathogen Campylobacter, jejuni reveals an elongated hexamer with D3 symmetry compatible with the, dimeric 2C-methyl-D-erythritol-4-phosphate cytidylyltransferase and, trimeric 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase, monofunctional enzymes. Complex formation of IspDF with, 4-diphosphocytidyl-2C-methyl-D-erythritol kinase (IspE), the intervening, enzyme activity in the pathway, has been observed in solution for the, enzymes from C. jejuni and Agrobacterium tumefaciens. The monofunctional, enzymes (2C-methyl-D-erythritol-4-phosphate cytidylyltransferase, IspE, and 2C-methyl-D-erythritol-2,4-cyclodiphosphate synthase) involved in the, DOXP biosynthetic pathway of Escherichia coli also show physical, associations. We propose that complex formation of the three enzymes at, the core of the DOXP pathway can produce an assembly localizing 18, catalytic centers for the early stages of isoprenoid biosynthesis.
About this Structure
1W57 is a Single protein structure of sequence from Campylobacter jejuni with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Hexameric assembly of the bifunctional methylerythritol 2,4-cyclodiphosphate synthase and protein-protein associations in the deoxy-xylulose-dependent pathway of isoprenoid precursor biosynthesis., Gabrielsen M, Bond CS, Hallyburton I, Hecht S, Bacher A, Eisenreich W, Rohdich F, Hunter WN, J Biol Chem. 2004 Dec 10;279(50):52753-61. Epub 2004 Oct 2. PMID:15466439
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