This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2eg7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2eg7.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2eg7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2eg7| PDB=2eg7 | SCENE= }}
{{STRUCTURE_2eg7| PDB=2eg7 | SCENE= }}
-
'''The crystal structure of E. coli dihydroorotase complexed with HDDP'''
+
===The crystal structure of E. coli dihydroorotase complexed with HDDP===
-
==Overview==
+
<!--
-
Dihydroorotase (DHOase) catalyzes the reversible cyclization of N-carbamyl-L-aspartate (CA-asp) to L-dihydroorotate (DHO) in the de novo biosynthesis of pyrimidine nucleotides. DHOase is a potential anti-malarial drug target as malarial parasites can only synthesize pyrimidines via the de novo pathway and do not possess a salvage pathway. Here we report the structures of Escherichia coli DHOase crystallized without ligand (1.7 A resolution) and in the presence of the inhibitors 2-oxo-1,2,3,6-tetrahydropyrimidine-4,6-dicarboxylate (HDDP; 2.0 A) and 5-fluoroorotate (FOA, 2.2 A). These are the first crystal structures of DHOase-inhibitor complexes, providing structural information on the mode of inhibitor binding. HDDP possesses features of both the substrate and product, and ligates the Zn atoms in the active site. In addition, HDDP forms hydrogen bonds to the flexible loop (residues 105-115) stabilizing the "loop-in" conformation of the flexible loop normally associated with the presence of CA-asp in the active site. By contrast, FOA, a product-like inhibitor, binds to the active site in a similar fashion to DHO but does not ligate the Zn atoms directly nor stabilize the loop-in conformation. These structures define the necessary features for the future design of improved inhibitors of DHOase.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17550785}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17550785 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17550785}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Amidohydrolase]]
[[Category: Amidohydrolase]]
[[Category: Tim barrel]]
[[Category: Tim barrel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:30:07 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:00:41 2008''

Revision as of 11:00, 29 July 2008

Image:2eg7.png

Template:STRUCTURE 2eg7

The crystal structure of E. coli dihydroorotase complexed with HDDP

Template:ABSTRACT PUBMED 17550785

About this Structure

2EG7 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structures of ligand-free and inhibitor complexes of dihydroorotase from Escherichia coli: implications for loop movement in inhibitor design., Lee M, Chan CW, Graham SC, Christopherson RI, Guss JM, Maher MJ, J Mol Biol. 2007 Jul 27;370(5):812-25. Epub 2007 May 22. PMID:17550785

Page seeded by OCA on Tue Jul 29 14:00:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2eg7"
Personal tools