1tm5
crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 M59A mutant
|
OverviewOverview
A series of mutants of chymotrypsin inhibitor 2 (CI2), at residues that, interact with the inhibited enzyme subtilisin BPN', were studied to, determine the relative importance of intermolecular contacts on either, side of the scissile bond. Mutants were tested for inhibition of, subtilisin, rates of hydrolysis by subtilisin, and ability to acylate, subtilisin. Additionally, crystal structures of the mutant CI2 complexes, with subtilisin were obtained. Ordered water molecules were found to play, an important role in inhibitor recognition, and features of the crystal, structures, in combination with biochemical data, support a, transition-state stabilization role for the P(1) residue in subtilisin, catalysis. Consistent with the proposed mechanism of inhibition, in which, rapid acylation is followed by religation, leaving-group contacts with the, enzyme were found to be more critical determinants of inhibition than, acylating-group contacts in the mutants studied here.
About this StructureAbout this Structure
1TM5 is a Protein complex structure of sequences from Bacillus amyloliquefaciens and Hordeum vulgare subsp. vulgare with CA, NA, CIT and 1PE as ligands. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.
ReferenceReference
Binding, proteolytic, and crystallographic analyses of mutations at the protease-inhibitor interface of the subtilisin BPN'/chymotrypsin inhibitor 2 complex., Radisky ES, Kwan G, Karen Lu CJ, Koshland DE Jr, Biochemistry. 2004 Nov 2;43(43):13648-56. PMID:15504027
Page seeded by OCA on Wed Nov 21 03:24:09 2007