We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1dbt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1dbt.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1dbt.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1dbt| PDB=1dbt | SCENE= }}
{{STRUCTURE_1dbt| PDB=1dbt | SCENE= }}
-
'''CRYSTAL STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH UMP'''
+
===CRYSTAL STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH UMP===
-
==Overview==
+
<!--
-
The crystal structure of Bacillus subtilis orotidine 5'-monophosphate (OMP) decarboxylase with bound uridine 5'-monophosphate has been determined by multiple wavelength anomalous diffraction phasing techniques and refined to an R-factor of 19.3% at 2.4 A resolution. OMP decarboxylase is a dimer of two identical subunits. Each monomer consists of a triosephosphate isomerase barrel and contains an active site that is located across one end of the barrel and near the dimer interface. For each active site, most of the residues are contributed by one monomer with a few residues contributed from the adjacent monomer. The most highly conserved residues are located in the active site and suggest a novel catalytic mechanism for decarboxylation that is different from any previously proposed OMP decarboxylase mechanism. The uridine 5'-monophosphate molecule is bound to the active site such that the phosphate group is most exposed and the C5-C6 edge of the pyrimidine base is most buried. In the proposed catalytic mechanism, the ground state of the substrate is destabilized by electrostatic repulsion between the carboxylate of the substrate and the carboxylate of Asp60. This repulsion is reduced in the transition state by shifting negative charge from the carboxylate to C6 of the pyrimidine, which is close to the protonated amine of Lys62. We propose that the decarboxylation of OMP proceeds by an electrophilic substitution mechanism in which decarboxylation and carbon-carbon bond protonation by Lys62 occur in a concerted reaction.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10681442}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10681442 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10681442}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Tim barrel]]
[[Category: Tim barrel]]
[[Category: Ump]]
[[Category: Ump]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:40:02 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:47:34 2008''

Revision as of 19:47, 30 June 2008

Image:1dbt.png

Template:STRUCTURE 1dbt

CRYSTAL STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM BACILLUS SUBTILIS COMPLEXED WITH UMP

Template:ABSTRACT PUBMED 10681442

About this Structure

1DBT is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

The crystal structure and mechanism of orotidine 5'-monophosphate decarboxylase., Appleby TC, Kinsland C, Begley TP, Ealick SE, Proc Natl Acad Sci U S A. 2000 Feb 29;97(5):2005-10. PMID:10681442

Page seeded by OCA on Mon Jun 30 22:47:34 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dbt"
Personal tools