1hyt
From Proteopedia
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RE-DETERMINATION AND REFINEMENT OF THE COMPLEX OF BENZYLSUCCINIC ACID WITH THERMOLYSIN AND ITS RELATION TO THE COMPLEX WITH CARBOXYPEPTIDASE A
Overview
The complex of benzylsuccinic acid with thermolysin has been redetermined, at 1.7-A resolution and refined to a crystallographic residual of 15.7%., In contrast to the prior study, which was to 2.3-A resolution, and without, the benefit of refinement (Bolognesi, M. C. and Matthews, B. W. (1979) J., Biol. Chem. 254, 634-639), the present analysis shows that it is the D-, rather than the L-isomer of benzylsuccinic acid that binds. The, stereochemistry of the zinc-carboxylate interaction is now seen to be syn, as is also observed in all known zinc-carboxylate complexes of both, thermolysin and carboxypeptidase A. The mode of binding of the, beta-carboxylate resembles the presumed geometry of the tetrahedral, transition state and, as such, is consistent with the commonly accepted, mechanism of action of thermolysin and of carboxypeptidase A.
About this Structure
1HYT is a Single protein structure of sequence from Bacillus thermoproteolyticus with CA, ZN, DMS and BZS as ligands. Active as Thermolysin, with EC number 3.4.24.27 Full crystallographic information is available from OCA.
Reference
Redetermination and refinement of the complex of benzylsuccinic acid with thermolysin and its relation to the complex with carboxypeptidase A., Hausrath AC, Matthews BW, J Biol Chem. 1994 Jul 22;269(29):18839-42. PMID:8034637
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