1lor: Difference between revisions
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'''crystal structure of orotidine 5'-monophosphate complexed with BMP''' | '''crystal structure of orotidine 5'-monophosphate complexed with BMP''' | ||
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[[Category: Pai, E F.]] | [[Category: Pai, E F.]] | ||
[[Category: Wu, N.]] | [[Category: Wu, N.]] | ||
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:07:38 2008'' | |||
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Revision as of 21:07, 2 May 2008
crystal structure of orotidine 5'-monophosphate complexed with BMP
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
1LOR is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. 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 Page seeded by OCA on Sat May 3 00:07:38 2008
