1lor: Difference between revisions

Revision as of 21:38, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1lor.png

Template:STRUCTURE 1lor

crystal structure of orotidine 5'-monophosphate complexed with BMPcrystal structure of orotidine 5'-monophosphate complexed with BMP

Template:ABSTRACT PUBMED 12011084

About this StructureAbout this Structure

1LOR is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.

ReferenceReference

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 Wed Jul 2 21:37:59 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''crystal structure of orotidine 5'-monophosphate complexed with BMP'''
+===crystal structure of orotidine 5'-monophosphate complexed with BMP===
-==Overview==
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-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.
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+{{ABSTRACT_PUBMED_12011084}}
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