1w55: Difference between revisions

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.

1W55 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni] with MG, C, GPP and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W55 OCA].  

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