1dv7
From Proteopedia
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| - | [[Image:1dv7.gif|left|200px]] | + | [[Image:1dv7.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF OROTIDINE MONOPHOSPHATE DECARBOXYLASE''' | + | {{Structure |
| + | |PDB= 1dv7 |SIZE=350|CAPTION= <scene name='initialview01'>1dv7</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF OROTIDINE MONOPHOSPHATE DECARBOXYLASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DV7 is a [ | + | 1DV7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DV7 OCA]. |
==Reference== | ==Reference== | ||
| - | Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase., Wu N, Mo Y, Gao J, Pai EF, Proc Natl Acad Sci U S A. 2000 Feb 29;97(5):2017-22. PMID:[http:// | + | Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase., Wu N, Mo Y, Gao J, Pai EF, Proc Natl Acad Sci U S A. 2000 Feb 29;97(5):2017-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10681441 10681441] |
[[Category: Methanothermobacter thermautotrophicus]] | [[Category: Methanothermobacter thermautotrophicus]] | ||
[[Category: Orotidine-5'-phosphate decarboxylase]] | [[Category: Orotidine-5'-phosphate decarboxylase]] | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:44:53 2008'' |
Revision as of 08:44, 20 March 2008
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| , resolution 1.80Å | |||||||
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| Activity: | Orotidine-5'-phosphate decarboxylase, with EC number 4.1.1.23 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF OROTIDINE MONOPHOSPHATE DECARBOXYLASE
Overview
Orotidine 5'-monophosphate decarboxylase catalyzes the conversion of orotidine 5'-monophosphate to uridine 5'-monophosphate, the last step in biosynthesis of pyrimidine nucleotides. As part of a Structural Genomics Initiative, the crystal structures of the ligand-free and the6-azauridine 5'-monophosphate-complexed forms have been determined at 1.8 and 1.5 A, respectively. The protein assumes a TIM-barrel fold with one side of the barrel closed off and the other side binding the inhibitor. A unique array of alternating charges (Lys-Asp-Lys-Asp) in the active site prompted us to apply quantum mechanical and molecular dynamics calculations to analyze the relative contributions of ground state destabilization and transition state stabilization to catalysis. The remarkable catalytic power of orotidine 5'-monophosphate decarboxylase is almost exclusively achieved via destabilization of the reactive part of the substrate, which is compensated for by strong binding of the phosphate and ribose groups. The computational results are consistent with a catalytic mechanism that is characterized by Jencks's Circe effect.
About this Structure
1DV7 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.
Reference
Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase., Wu N, Mo Y, Gao J, Pai EF, Proc Natl Acad Sci U S A. 2000 Feb 29;97(5):2017-22. PMID:10681441
Page seeded by OCA on Thu Mar 20 10:44:53 2008
