2pmp
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(New page: 200px<br /><applet load="2pmp" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pmp, resolution 2.300Å" /> '''Structure of 2C-met...)
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Revision as of 11:35, 23 January 2008
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Structure of 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase from the isoprenoid biosynthetic pathway of Arabidopsis thaliana
Overview
The X-ray crystal structure of the 2C-methyl-d-erythritol, 2,4-cyclodiphosphate synthase (MCS) from Arabidopsis thaliana has been, solved at 2.3 A resolution in complex with a cytidine-5-monophosphate, (CMP) molecule. This is the first structure determined of an MCS enzyme, from a plant. Major differences between the A. thaliana and bacterial MCS, structures are found in the large molecular cavity that forms between, subunits and involve residues that are highly conserved among plants. In, some bacterial enzymes, the corresponding cavity has been shown to be an, isoprenoid diphosphate-like binding pocket, with a proposed, feedback-regulatory role. Instead, in the structure from A. thaliana the, cavity is unsuited for binding a diphosphate moiety, which suggests a, different regulatory mechanism of MCS enzymes between bacteria and plants.
About this Structure
2PMP is a Single protein structure of sequence from Arabidopsis thaliana with , , and as ligands. Active as 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, with EC number 4.6.1.12 Full crystallographic information is available from OCA.
Reference
Biosynthesis of isoprenoids in plants: Structure of the 2C-methyl-D-erithrytol 2,4-cyclodiphosphate synthase from Arabidopsis thaliana. Comparison with the bacterial enzymes., Calisto BM, Perez-Gil J, Bergua M, Querol-Audi J, Fita I, Imperial S, Protein Sci. 2007 Sep;16(9):2082-8. Epub 2007 Jul 27. PMID:17660251
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