1HYT: Re-determination and Refinement of the Complex of Benzylsuccinic Acid With Thermolysin and ITS Relation to the Complex With Carboxypeptidase a

Citation:
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.
PDB ID: 1HYTDownload
MMDB ID: 56397
PDB Deposition Date: 1994/5/4
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 1.7  Å
Source Organism:
Similar Structures:
Biological Unit for 1HYT: dimeric; determined by author and by software (PISA)
Molecular Components in 1HYT
Label Count Molecule
Proteins (2 molecules)
2
Thermolysin
Molecule annotation
Chemicals (14 molecules)
1
8
2
2
3
2
4
2
* Click molecule labels to explore molecular sequence information.

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