1HYT

RE-DETERMINATION AND REFINEMENT OF THE COMPLEX OF BENZYLSUCCINIC ACID WITH THERMOLYSIN AND ITS RELATION TO THE COMPLEX WITH CARBOXYPEPTIDASE A

Summary for 1HYT

• Entry DOI: 10.2210/pdb1hyt/pdb
• Descriptor: THERMOLYSIN, CALCIUM ION, ZINC ION, ... (6 entities in total)
• Functional Keywords: hydrolase(metalloproteinase)
• Biological source: Bacillus thermoproteolyticus
• Cellular location: Secreted: P00800
• Total number of polymer chains: 1
• Total formula weight: 34874.37

Authors

Hausrath, A.C.,Matthews, B.W. (deposition date: 1994-05-04, release date: 1994-07-31, Last modification date: 2024-02-07)

Primary citation

Hausrath, A.C.,Matthews, B.W.
Redetermination and refinement of the complex of benzylsuccinic acid with thermolysin and its relation to the complex with carboxypeptidase A.
J.Biol.Chem., 269:18839-18842, 1994

PubMed Abstract: 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.

PubMed: 8034637

Experimental method

X-RAY DIFFRACTION (1.7 Å)