1dv7: Difference between revisions

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[[Image:1dv7.gif|left|200px]]
[[Image:1dv7.gif|left|200px]]


{{Structure
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|PDB= 1dv7 |SIZE=350|CAPTION= <scene name='initialview01'>1dv7</scene>, resolution 1.80&Aring;
The line below this paragraph, containing "STRUCTURE_1dv7", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND=
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[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] </span>
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{{STRUCTURE_1dv7| PDB=1dv7  | SCENE= }}  
|RELATEDENTRY=[[1dvj|1DVJ]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dv7 OCA], [http://www.ebi.ac.uk/pdbsum/1dv7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dv7 RCSB]</span>
}}


'''CRYSTAL STRUCTURE OF OROTIDINE MONOPHOSPHATE DECARBOXYLASE'''
'''CRYSTAL STRUCTURE OF OROTIDINE MONOPHOSPHATE DECARBOXYLASE'''
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[[Category: Pai, E F.]]
[[Category: Pai, E F.]]
[[Category: Wu, N.]]
[[Category: Wu, N.]]
[[Category: dimer]]
[[Category: Dimer]]
[[Category: lyase]]
[[Category: Lyase]]
[[Category: tim barrel]]
[[Category: Tim barrel]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:19:04 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:49:21 2008''

Revision as of 14:19, 2 May 2008

File:1dv7.gif


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


OverviewOverview

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 StructureAbout this Structure

1DV7 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.

ReferenceReference

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 Fri May 2 14:19:04 2008

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