1GCT

IS GAMMA-CHYMOTRYPSIN A TETRAPEPTIDE ACYL-ENZYME ADDUCT OF GAMMA-CHYMOTRYPSIN?

Summary for 1GCT

• Entry DOI: 10.2210/pdb1gct/pdb
• Related: 2GCT 3GCT
• Descriptor: GAMMA-CHYMOTRYPSIN A, TETRAPEPTIDE ADDUCT, SULFATE ION, ... (6 entities in total)
• Functional Keywords: hydrolase, serine proteinase, hydrolase-peptide complex, hydrolase/peptide
• Biological source: Bos taurus; More
• Cellular location: Secreted, extracellular space: P00766 P00766 P00766
• Total number of polymer chains: 4
• Total formula weight: 25850.16

Authors

Dixon, M.M.,Matthews, B.W. (deposition date: 1990-09-04, release date: 1991-10-15, Last modification date: 2024-10-30)

Primary citation

Dixon, M.M.,Matthews, B.W.
Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?
Biochemistry, 28:7033-7038, 1989

PubMed Abstract: Refinement of the structure of gamma-chymotrypsin based on X-ray crystallographic data to 1.6-A resolution has confirmed the overall conformation of the molecule as reported previously [Cohen, G. H., Silverton, E. W., & Davies, D. R. (1981) J. Mol. Biol. 148, 449-479]. In addition, the new refinement suggests that gamma-chymotrypsin, which is operationally defined by its crystalline habit, may not be the free enzyme but rather a complex, possibly an acyl-enzyme adduct, with the tetrapeptide Pro-Gly-Ala-Tyr (or a close homologue). The crystallographic refinement provides a detailed geometrical description of the enzyme-substrate-solvent interactions that occur in the presumptive adduct.

PubMed: 2819046
DOI: 10.1021/bi00443a038

Experimental method

X-RAY DIFFRACTION (1.6 Å)