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Biology (Basel). 2021 Oct 09;10(10). doi: 10.3390/biology10101021.

First Crystal Structure of Bacterial Oligopeptidase B in an Intermediate State: The Roles of the Hinge Region Modification and Spermine.

Biology

Dmitry E Petrenko, Vladimir I Timofeev, Vladimir V Britikov, Elena V Britikova, Sergey Y Kleymenov, Anna V Vlaskina, Inna P Kuranova, Anna G Mikhailova, Tatiana V Rakitina

Affiliations

  1. National Research Center "Kurchatov Institute", 123182 Moscow, Russia.
  2. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, RAS, 117997 Moscow, Russia.
  3. Federal Scientific Research Center "Crystallography and Photonics", RAS, 119333 Moscow, Russia.
  4. Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, 220141 Minsk, Belarus.
  5. Bach Institute of Biochemistry, Federal Research Center "Fundamentals of Biotechnology", RAS, 119071 Moscow, Russia.
  6. Koltzov Institute of Developmental Biology, RAS, 119334 Moscow, Russia.

PMID: 34681120 PMCID: PMC8533160 DOI: 10.3390/biology10101021

Abstract

Oligopeptidase B (OpB) is a two-domain, trypsin-like serine peptidase belonging to the S9 prolyloligopeptidase (POP) family. Two domains are linked by a hinge region that participates in the transition of the enzyme between two major states-closed and open-in which domains and residues of the catalytic triad are located close to each other and separated, respectively. In this study, we described, for the first time, a structure of OpB from bacteria obtained for an enzyme from

Keywords: Serratia proteomaculans; crystal structure; hinge region; intermediate state; oligopeptidase B; prolyloligopeptidase; small-angle X-ray scattering; spermine

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