1l2u
From Proteopedia
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Orotidine 5'-monophosphate decarboxylase from E. coli
Overview
Orotidine 5'-monophosphate decarboxylase (ODCase) catalyses the, decarboxylation of orotidine 5'-monophosphate to uridine 5'-monophosphate, (UMP). We have earlier determined the structure of ODCase from Escherichia, coli complexed with the inhibitor, 1-(5'-phospho-beta-d-ribofuranosyl)barbituric acid (BMP); here we present, the 2.5 A structure of the uncomplexed apo enzyme, determined from twinned, crystals. A structural analysis and comparison of the two structures of, the E. coli enzyme show that binding of the inhibitor is accompanied by, significant domain movements of approximately 12 degrees around a hinge, that crosses the active site. Hence, the ODCase dimer, which contains two, active sites, may be divided in three domains: a central domain that is, fixed, and two lids which independently move 12 degrees upon binding., Corresponding analyses, presented herein, of the two Saccharomyces, cerevisiae ODCase structures (with and without BMP) and the, Methanobacterium thermoautotrophicum ODCase structures (with and without, 6-aza UMP) show very similar, but somewhat smaller domain movements. The, domain movements seem to be initiated by the phosphoryl binding to the, enzyme and can explain why the binding of the phosphoryl group is, essential for the catalytic function.
About this Structure
1L2U is a Single protein structure of sequence from Escherichia coli. Active as Orotidine-5'-phosphate decarboxylase, with EC number 4.1.1.23 Full crystallographic information is available from OCA.
Reference
Substrate binding induces domain movements in orotidine 5'-monophosphate decarboxylase., Harris P, Poulsen JC, Jensen KF, Larsen S, J Mol Biol. 2002 May 10;318(4):1019-29. PMID:12054799
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