1LOR

crystal structure of orotidine 5'-monophosphate complexed with BMP

Summary for 1LOR

• Entry DOI: 10.2210/pdb1lor/pdb
• Related: 1LOL 1LOQ 1LOS 1LP6
• Descriptor: orotidine monophosphate decarboxylase, 6-HYDROXYURIDINE-5'-PHOSPHATE (3 entities in total)
• Functional Keywords: tim barrel, lyase
• Biological source: Methanothermobacter thermautotrophicus
• Total number of polymer chains: 1
• Total formula weight: 25206.84

Authors

Wu, N.,Pai, E.F. (deposition date: 2002-05-06, release date: 2002-08-07, Last modification date: 2024-02-14)

Primary citation

Wu, N.,Pai, E.F.
Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase.
J.Biol.Chem., 277:28080-28087, 2002

PubMed Abstract: 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.

PubMed: 12011084
DOI: 10.1074/jbc.M202362200

Experimental method

X-RAY DIFFRACTION (1.6 Å)