1loq
From Proteopedia
(New page: 200px<br /><applet load="1loq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1loq, resolution 1.50Å" /> '''Crystal structure of...) |
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| - | [[Image:1loq.jpg|left|200px]]<br /><applet load="1loq" size=" | + | [[Image:1loq.jpg|left|200px]]<br /><applet load="1loq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1loq, resolution 1.50Å" /> | caption="1loq, resolution 1.50Å" /> | ||
'''Crystal structure of orotidine monophosphate decarboxylase complexed with product UMP'''<br /> | '''Crystal structure of orotidine monophosphate decarboxylase complexed with product UMP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structures of the enzyme orotidine-5'-monophosphate | + | 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== | ==About this Structure== | ||
| - | 1LOQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with U as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23] Full crystallographic information is available from [http:// | + | 1LOQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=U:'>U</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Orotidine-5'-phosphate decarboxylase]] | [[Category: Orotidine-5'-phosphate decarboxylase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Pai, E | + | [[Category: Pai, E F.]] |
[[Category: Wu, N.]] | [[Category: Wu, N.]] | ||
[[Category: U]] | [[Category: U]] | ||
[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:56 2008'' |
Revision as of 11:46, 21 February 2008
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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 of sequence from [1] with as ligand. Active as Orotidine-5'-phosphate decarboxylase, with EC number 4.1.1.23 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 [[Category: ]]
Page seeded by OCA on Thu Feb 21 13:46:56 2008
