1lp6

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{{STRUCTURE_1lp6| PDB=1lp6 | SCENE= }}
{{STRUCTURE_1lp6| PDB=1lp6 | SCENE= }}
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'''Crystal structure of orotidine monophosphate decarboxylase complexed with CMP'''
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===Crystal structure of orotidine monophosphate decarboxylase complexed with CMP===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 12011084 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12011084}}
==About this Structure==
==About this Structure==
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[[Category: Wu, N.]]
[[Category: Wu, N.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 21:41:12 2008''

Revision as of 18:41, 2 July 2008

Image:1lp6.png

Template:STRUCTURE 1lp6

Crystal structure of orotidine monophosphate decarboxylase complexed with CMP

Template:ABSTRACT PUBMED 12011084

About this Structure

1LP6 is a Single protein structure. 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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