2C57

H.pylori type II dehydroquinase in complex with FA1

Summary for 2C57

• Entry DOI: 10.2210/pdb2c57/pdb
• Related: 1J2Y 2C4V 2C4W
• Descriptor: 3-DEHYDROQUINATE DEHYDRATASE, 2,3 -ANHYDRO-QUINIC ACID (2 entities in total)
• Functional Keywords: dehydroquinase, dehydroquinate, sulphonamide, lyase, 3-dehydroquinase, shikimate pathway, aromatic amino acid biosynthesis
• Biological source: HELICOBACTER PYLORI
• Total number of polymer chains: 12
• Total formula weight: 241594.39

Authors

Robinson, D.A.,Lapthorn, A.J. (deposition date: 2005-10-26, release date: 2006-02-22, Last modification date: 2023-12-13)

Primary citation

Robinson, D.A.,Stewart, K.A.,Price, N.C.,Chalk, P.A.,Coggins, J.R.,Lapthorn, A.J.
Crystal Structures of Helicobacter Pylori Type II Dehydroquinase Inhibitor Complexes: New Directions for Inhibitor Design.
J.Med.Chem., 49:1282-, 2006

PubMed Abstract: 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.

PubMed: 16480265
DOI: 10.1021/JM0505361

Experimental method

X-RAY DIFFRACTION (3.1 Å)