The β-propeller domain of the trilobed protease from Pyrococcus furiosus reveals an open Velcro topology

Jürgen Bosch, Tomohiro Tamura, Noriko Tamura, Wolfgang Baumeister, Lars Oliver Essen

Research output: Contribution to journalArticle

Abstract

In the proteolytic pathway of prokaryotic and eukaryotic organisms, proteins tagged for proteolysis are firstly shredded into smaller peptides by compartmentalized proteases such as the proteasome complex. Accordingly, a variety of downstream proteases have evolved to further hydrolyze these peptides to the level of free amino acids. In the search for such downstream proteases, a high-molecular-weight protease complex called trilobed protease (TLP) was recently discovered in the archaeon Pyroccocus furiosus. The crystal structure of the N-terminal β-propeller domain of the trilobed protease at 2 Å resolution shows that the trilobed protease utilizes this accessory domain to control substrate access to the active site. Modelling of the intact TLP monomer suggests that this protease has an additional side entrance to its active site as in the DPP-IV or tricorn protease complexes.

Original languageEnglish (US)
Pages (from-to)179-187
Number of pages9
JournalActa Crystallographica Section D: Biological Crystallography
Volume63
Issue number2
DOIs
StatePublished - Feb 2007
Externally publishedYes

    Fingerprint

Keywords

  • β-propeller domain structures
  • Archaeal proteases
  • Tricorn

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this