1oj4: Difference between revisions
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Revision as of 16:51, 30 October 2007
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TERNARY COMPLEX OF 4-DIPHOSPHOCYTIDYL-2-C-METHYL-D-ERYTHRITOL KINASE
OverviewOverview
4-Diphosphocytidyl-2C-methyl-d-erythritol kinase, an essential enzyme in, the nonmevalonate pathway of isopentenyl diphosphate and dimethylallyl, diphosphate biosynthesis, catalyzes the single ATP-dependent, phosphorylation stage affording, 4-diphosphocytidyl-2C-methyl-d-erythritol-2-phosphate. The 2-A resolution, crystal structure of the Escherichia coli enzyme in a ternary complex with, substrate and a nonhydrolyzable ATP analogue reveals the molecular, determinants of specificity and catalysis. The enzyme subunit displays the, alpha/beta fold characteristic of the galactose kinase/homoserine, kinase/mevalonate kinase/phosphomevalonate kinase superfamily, arranged, into cofactor and substrate-binding domains with the catalytic center, positioned in a deep cleft between domains. ... [(full description)]
About this StructureAbout this Structure
1OJ4 is a [Single protein] structure of sequence from [Escherichia coli] with CL, CDM and ANP as [ligands]. Active as [4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase], with EC number [2.7.1.148]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Biosynthesis of isoprenoids: crystal structure of 4-diphosphocytidyl-2C-methyl-D-erythritol kinase., Miallau L, Alphey MS, Kemp LE, Leonard GA, McSweeney SM, Hecht S, Bacher A, Eisenreich W, Rohdich F, Hunter WN, Proc Natl Acad Sci U S A. 2003 Aug 5;100(16):9173-8. Epub 2003 Jul 23. PMID:12878729
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