2TRM

THE THREE-DIMENSIONAL STRUCTURE OF ASN102 MUTANT OF TRYPSIN. ROLE OF ASP102 IN SERINE PROTEASE CATALYSIS

Summary for 2TRM

• Entry DOI: 10.2210/pdb2trm/pdb
• Descriptor: TRYPSIN, CALCIUM ION, BENZAMIDINE, ... (4 entities in total)
• Functional Keywords: hydrolase (serine proteinase)
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Secreted, extracellular space: P00763
• Total number of polymer chains: 1
• Total formula weight: 23974.08

Authors

Stroud, R.M.,Finer-Moore, J. (deposition date: 1988-04-25, release date: 1988-07-16, Last modification date: 2017-11-29)

Primary citation

Sprang, S.,Standing, T.,Fletterick, R.J.,Stroud, R.M.,Finer-Moore, J.,Xuong, N.H.,Hamlin, R.,Rutter, W.J.,Craik, C.S.
The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis.
Science, 237:905-909, 1987

PubMed Abstract: The structure of the Asn102 mutant of trypsin was determined in order to distinguish whether the reduced activity of the mutant at neutral pH results from an altered active site conformation or from an inability to stabilize a positive charge on the active site histidine. The active site structure of the Asn102 mutant of trypsin is identical to the native enzyme with respect to the specificity pocket, the oxyanion hole, and the orientation of the nucleophilic serine. The observed decrease in rate results from the loss of nucleophilicity of the active site serine. This decreased nucleophilicity may result from stabilization of a His57 tautomer that is unable to accept the serine hydroxyl proton.

PubMed: 3112942

Experimental method

X-RAY DIFFRACTION (2.8 Å)