1YKT

Trypsin/Bpti complex mutant

Summary for 1YKT

• Entry DOI: 10.2210/pdb1ykt/pdb
• Descriptor: Trypsin II, Pancreatic trypsin inhibitor, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: bpti, trypsin, mutant, hydrolase
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Secreted, extracellular space: P00763; Secreted: P00974
• Total number of polymer chains: 2
• Total formula weight: 30430.48

Authors

Brown, C.K.,Ohlendorf, D.H. (deposition date: 2005-01-18, release date: 2006-04-25, Last modification date: 2024-10-30)

Primary citation

Getun, I.V.,Brown, C.K.,Tulla-Puche, J.,Ohlendorf, D.,Woodward, C.,Barany, G.
Partially folded bovine pancreatic trypsin inhibitor analogues attain fully native structures when co-crystallized with S195A rat trypsin
J.Mol.Biol., 375:812-823, 2008

PubMed Abstract: Crystal structures, at 1.7 A resolution, were solved for complexes between each of two chemically synthesized partially folded analogues of bovine pancreatic trypsin inhibitor (BPTI) with the proteolytically inactive rat trypsin mutant S195A. The BPTI analogue termed [14-38](Abu) retains only the disulfide bond between Cys14 and Cys38, while Cys5, Cys30, Cys51, and Cys55 are replaced by isosteric alpha-amino-n-butyric acid residues. The analogue K26P,A27D[14-38](Abu) contains two further replacements, by statistically favored residues, in the type I beta-turn that has been suggested to be a main site for initiation of BPTI folding. As a control, the structure of the complex between S195A trypsin and wild-type BPTI was also solved. Despite significant differences in the degree of structure detected among these three BPTIs in solution by several biophysical techniques, their tertiary folds once bound to S195A trypsin in a crystalline lattice are essentially superimposable.

PubMed: 18054043
DOI: 10.1016/j.jmb.2007.10.084

Experimental method

X-RAY DIFFRACTION (1.7 Å)