1ot5

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spinqualitylabelsall models 1ot5, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

The 2.4 Angstrom Crystal Sructure of Kex2 in complex with a peptidyl-boronic acid inhibitor

Overview

This paper reports the first structure of a member of the Kex2/furin family of eukaryotic pro-protein processing proteases, which cleave sites consisting of pairs or clusters of basic residues. Reported is the 2.4 A resolution crystal structure of the two-domain protein ssKex2 in complex with an Ac-Ala-Lys-boroArg inhibitor (R = 20.9%, R(free) = 24.5%). The Kex2 proteolytic domain is similar in its global fold to the subtilisin-like superfamily of degradative proteases. Analysis of the complex provides a structural basis for the extreme selectivity of this enzyme family that has evolved from a nonspecific subtilisin-like ancestor. The P-domain of ssKex2 has a novel jelly roll like fold consisting of nine beta strands and may potentially be involved, along with the buried Ca(2+) ion, in creating the highly determined binding site for P(1) arginine.

About this Structure

1OT5 is a Single protein structure of sequence from Saccharomyces cerevisiae with , and as ligands. Active as Kexin, with EC number 3.4.21.61 Full crystallographic information is available from OCA.

Reference

2.4 A resolution crystal structure of the prototypical hormone-processing protease Kex2 in complex with an Ala-Lys-Arg boronic acid inhibitor., Holyoak T, Wilson MA, Fenn TD, Kettner CA, Petsko GA, Fuller RS, Ringe D, Biochemistry. 2003 Jun 10;42(22):6709-18. PMID:12779325

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