1lor: Difference between revisions

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New page: left|200px<br /><applet load="1lor" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lor, resolution 1.60Å" /> '''crystal structure of...
 
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[[Image:1lor.jpg|left|200px]]<br /><applet load="1lor" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1lor.jpg|left|200px]]<br /><applet load="1lor" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1lor, resolution 1.60&Aring;" />
caption="1lor, resolution 1.60&Aring;" />
'''crystal structure of orotidine 5'-monophosphate complexed with BMP'''<br />
'''crystal structure of orotidine 5'-monophosphate complexed with BMP'''<br />


==Overview==
==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.
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==
1LOR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with BMP 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LOR OCA].  
1LOR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with <scene name='pdbligand=BMP:'>BMP</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=1LOR 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.F.]]
[[Category: Pai, E F.]]
[[Category: Wu, N.]]
[[Category: Wu, N.]]
[[Category: BMP]]
[[Category: BMP]]
[[Category: tim barrel]]
[[Category: tim barrel]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:44:06 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:46:55 2008''

Revision as of 14:46, 21 February 2008

File:1lor.jpg


1lor, resolution 1.60Å

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crystal structure of orotidine 5'-monophosphate complexed with BMP

OverviewOverview

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 StructureAbout this Structure

1LOR is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with as ligand. Active as Orotidine-5'-phosphate decarboxylase, with EC number 4.1.1.23 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

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