1loq
From Proteopedia
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[[Image:1loq.jpg|left|200px]] | [[Image:1loq.jpg|left|200px]] | ||
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'''Crystal structure of orotidine monophosphate decarboxylase complexed with product UMP''' | '''Crystal structure of orotidine monophosphate decarboxylase complexed with product UMP''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LOQ is a [[Single protein]] structure | + | 1LOQ is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOQ OCA]. |
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/12011084 12011084] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12011084 12011084] | ||
| - | [[Category: ]] | ||
[[Category: Orotidine-5'-phosphate decarboxylase]] | [[Category: Orotidine-5'-phosphate decarboxylase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Pai, E F.]] | [[Category: Pai, E F.]] | ||
[[Category: Wu, N.]] | [[Category: Wu, N.]] | ||
| - | [[Category: | + | [[Category: Tim barrel]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:07:36 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:07, 2 May 2008
Crystal structure of orotidine monophosphate decarboxylase complexed with product UMP
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
1LOQ 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 Page seeded by OCA on Sat May 3 00:07:36 2008
