1dv7

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{{STRUCTURE_1dv7| PDB=1dv7 | SCENE= }}
{{STRUCTURE_1dv7| PDB=1dv7 | SCENE= }}
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'''CRYSTAL STRUCTURE OF OROTIDINE MONOPHOSPHATE DECARBOXYLASE'''
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===CRYSTAL STRUCTURE OF OROTIDINE MONOPHOSPHATE DECARBOXYLASE===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_10681441}}
==About this Structure==
==About this Structure==
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[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Tim barrel]]
[[Category: Tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:40:00 2008''

Revision as of 20:40, 30 June 2008

Image:1dv7.png


PDB ID 1dv7

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1dv7, resolution 1.80Å ()
Activity: Orotidine-5'-phosphate decarboxylase, with EC number 4.1.1.23
Related: 1dvj
Resources: FirstGlance, OCA, RCSB, PDBsum, TOPSAN
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF OROTIDINE MONOPHOSPHATE DECARBOXYLASE

Template:ABSTRACT PUBMED 10681441

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

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