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The structure of endothiapepsin complexed with a Phe‐Tyr reduced‐bond inhibitor at 1.35 Å resolution
Author(s) -
Guo J.,
Cooper J. B.,
Wood S. P.
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x13032974
Subject(s) - active site , chemistry , hydrogen bond , peptide bond , stereochemistry , oligopeptide , enzyme , enzyme inhibitor , crystal structure , peptide , crystallography , biochemistry , organic chemistry , molecule
Endothiapepsin is a typical member of the aspartic proteinase family. The catalytic mechanism of this family is attributed to two conserved catalytic aspartate residues, which coordinate the hydrolysis of a peptide bond. An oligopeptide inhibitor (IC 50 = 0.62 µ M ) based on a reduced‐bond transition‐state inhibitor of mucorpepsin was co‐crystallized with endothiapepsin and the crystal structure of the enzyme–inhibitor complex was determined at 1.35 Å resolution. A total of 12 hydrogen bonds between the inhibitor and the active‐site residues were identified. The resulting structure demonstrates a number of novel subsite interactions in the active‐site cleft.