4XOJ

Structure of bovine trypsin in complex with analogues of sunflower inhibitor 1 (SFTI-1)

Summary for 4XOJ

• Entry DOI: 10.2210/pdb4xoj/pdb
• Descriptor: Cationic trypsin, Trypsin inhibitor 1, SULFATE ION, ... (8 entities in total)
• Functional Keywords: trypsin, sfti, inhibitor, splicing, protease, hydrolase
• Biological source: Bos taurus (Bovine); More
• Cellular location: Secreted, extracellular space: P00760
• Total number of polymer chains: 2
• Total formula weight: 27884.56

Authors

Golik, P.,Malicki, S.,Grudnik, P.,Karna, N.,Debowski, D.,Legowska, A.,Wladyka, B.,Gitlin, A.,Brzozowski, K.,Dubin, G.,Rolka, K. (deposition date: 2015-01-16, release date: 2015-08-12, Last modification date: 2024-10-09)

Primary citation

Karna, N.,Legowska, A.,Malicki, S.,Debowski, D.,Golik, P.,Gitlin, A.,Grudnik, P.,Wladyka, B.,Brzozowski, K.,Dubin, G.,Rolka, K.
Investigation of Serine-Proteinase-Catalyzed Peptide Splicing in Analogues of Sunflower Trypsin Inhibitor 1 (SFTI-1).
Chembiochem, 16:2036-2045, 2015

PubMed Abstract: Serine-proteinase-catalyzed peptide splicing was demonstrated in analogues of the trypsin inhibitor SFTI-1: both single peptides and two-peptide chains (C- and N-terminal peptide chains linked by a disulfide bridge). In the second series, peptide splicing with catalytic amount of proteinase was observed only when formation of acyl-enzyme intermediate was preceded by hydrolysis of the substrate Lys-Ser peptide bond. Here we demonstrate that with an equimolar amount of the proteinase, splicing occurs in all the two-peptide-chain analogues. This conclusion was supported by high resolution crystal structures of selected analogues in complex with trypsin. We showed that the process followed a direct transpeptidation mechanism. Thus, the acyl-enzyme intermediate was formed and was immediately used for a new peptide bond formation; products associated with the hydrolysis of the acyl-enzyme were not observed. The peptide splicing was sequence- not structure-specific.

PubMed: 26212347
DOI: 10.1002/cbic.201500296

Experimental method

X-RAY DIFFRACTION (0.91 Å)