2c57

From Proteopedia
Revision as of 20:00, 18 December 2007 by OCA (talk | contribs)
Jump to navigation Jump to search
File:2c57.gif


2c57, resolution 3.10Å

Drag the structure with the mouse to rotate

H.PYLORI TYPE II DEHYDROQUINASE IN COMPLEX WITH FA1

OverviewOverview

The crystal structures of the type II dehydroquinase (DHQase) from, Helicobacter pylori in complex with three competitive inhibitors have been, determined. The inhibitors are the substrate analogue 2,3-anhydroquinate, (FA1), citrate, and an oxoxanthene sulfonamide derivative (AH9095)., Despite the very different chemical nature of the inhibitors, in each case, the primary point of interaction with the enzyme is via the residues that, bind the C1 functionalities of the substrate, 3-dehydroquinate, i.e., N76, H102, I103, and H104. The DHQase/AH9095 complex crystal structure shows, that sulfonamides can form a scaffold for nonsubstrate-like inhibitors and, identifies a large conserved hydrophobic patch at the entrance to the, active site as a locus that can be exploited in the development of new, ligands.

About this StructureAbout this Structure

2C57 is a Single protein structure of sequence from Helicobacter pylori with FA1 as ligand. Active as 3-dehydroquinate dehydratase, with EC number 4.2.1.10 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of Helicobacter pylori type II dehydroquinase inhibitor complexes: new directions for inhibitor design., Robinson DA, Stewart KA, Price NC, Chalk PA, Coggins JR, Lapthorn AJ, J Med Chem. 2006 Feb 23;49(4):1282-90. PMID:16480265

Page seeded by OCA on Tue Dec 18 19:10:14 2007

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA