Project Details
Projekt
Structure and function of HxH metalloproteases
Applicant
Professor Dr. Matthias Bochtler
Subject Area
Metabolism, Biochemistry and Genetics of Microorganisms
Term
from 2004 to 2007
Project identifier
Deutsche Forschungsgemeinschaft (DFG) - Project number 5422790
Metalloproteases can often be recognised by the presence of a short conserved signature sequence containing two histidines. This characteristic motif is most typically HEXXH or HXXEH, but several classes of amidohydrolases have now been identified that contain an HxH motif. With the exception of urease-type amidohydrolases, HxH metalloproteases are not well characterized mechanistically, and even the identity of the metal, its ligands and coordination geometry are unknown in many cases. We propose (a) to express, purify and characterize a series of bacterial HxH proteases (b) to determine their structure by X-ray crystallography and (c) to synthesize phosphinic acid, phosphonate ester and hydroxamate based substrate analogues/inhibitors for mechanistic studies.
DFG Programme
Priority Programmes
