1dvj: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,615 edits
No edit summary
Line 1: Line 1:
[[Image:1dvj.jpg|left|200px]]
{{Seed}}
[[Image:1dvj.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dvj|  PDB=1dvj  |  SCENE=  }}  
{{STRUCTURE_1dvj|  PDB=1dvj  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF OROTIDINE MONOPHOSPHATE DECARBOXYLASE COMPLEXED WITH 6-AZAUMP'''
===CRYSTAL STRUCTURE OF OROTIDINE MONOPHOSPHATE DECARBOXYLASE COMPLEXED WITH 6-AZAUMP===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_10681441}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10681441 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10681441}}


==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Dimer]]
[[Category: Dimer]]
[[Category: Tim barrel]]
[[Category: Tim barrel]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:19:58 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:40:58 2008''

Revision as of 20:41, 30 June 2008

File:1dvj.png

Template:STRUCTURE 1dvj

CRYSTAL STRUCTURE OF OROTIDINE MONOPHOSPHATE DECARBOXYLASE COMPLEXED WITH 6-AZAUMP

Template:ABSTRACT PUBMED 10681441

About this Structure

1DVJ 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 Mon Jun 30 23:40:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1dvj&oldid=589358"