The structure of endothiapepsin complexed with a Phe-Tyr reduced-bond inhibitor at 1.35 Å resolution

J. Guo, J. B. Cooper, S. P. Wood

Research output: Contribution to journalArticlepeer-review

Abstract

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 (IC50 = 0.62 µM) 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.
Original languageEnglish
Pages (from-to)30-33
JournalActa Crystallographica Section F: Structural Biology Communications
Volume70
Issue number1
Early online date24 Dec 2013
DOIs
Publication statusPublished - 1 Jan 2014

Keywords

  • endothiapepsin
  • aspartic proteases
  • transition state
  • inhibitor

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