1los
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(New page: 200px<br /><applet load="1los" size="450" color="white" frame="true" align="right" spinBox="true" caption="1los, resolution 1.90Å" /> '''crystal structure of...)
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Revision as of 18:36, 20 November 2007
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crystal structure of orotidine monophosphate decarboxylase mutant deltaR203A complexed with 6-azaUMP
Overview
The crystal structures of the enzyme orotidine-5'-monophosphate, decarboxylase from Methanobacterium thermoautotrophicum complexed with its, product UMP and the inhibitors 6-hydroxyuridine 5'-phosphate (BMP), XMP, and CMP are reported. A mutant version of the protein, in which four, residues of the flexible phosphate-binding loop (180)Gly-Gly(190) were, removed and Arg(203) was replaced by alanine, was also analyzed. The XMP, and CMP complexes reveal a ligand-binding mode that is distinct from the, one identified previously with the aromatic rings located outside the, binding pocket. A potential pathway for ligand binding is discussed.
About this Structure
1LOS is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with UP6 as ligand. Active as Orotidine-5'-phosphate decarboxylase, with EC number 4.1.1.23 Full crystallographic information is available from OCA.
Reference
Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase., Wu N, Pai EF, J Biol Chem. 2002 Aug 2;277(31):28080-7. Epub 2002 May 13. PMID:12011084
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