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Related Experiment Video

Updated: Jul 10, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

Published on: May 13, 2020

Oligopeptidase B: a processing peptidase involved in pathogenesis.

Theresa H T Coetzer¹, J P Dean Goldring, Laura E J Huson

¹Biochemistry, School of Biochemistry, Genetics, Microbiology and Plant Pathology, University of KwaZulu-Natal (Pietermaritzburg campus), Private bag X01, Scottsville 3201, South Africa. coetzer@ukzn.ac.za

|November 22, 2007

Summary

Oligopeptidase B, a bacterial serine peptidase, uniquely cleaves peptides at basic amino acids. Its structure, function, and role in trypanosomosis highlight its potential as a drug target.

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Area of Science:

Biochemistry
Molecular Biology
Enzymology

Background:

Oligopeptidase B (OB) is a serine peptidase from the prolyl oligopeptidase family found in bacteria, protozoa, and plants.
Unlike other prolyl oligopeptidases, OB cleaves peptides at the carboxyl side of basic amino acid residues.

Purpose of the Study:

To review the structure-function properties of Oligopeptidase B.
To explore its physiological and pathological roles.
To assess its potential as a drug target.

Main Methods:

Molecular modeling and mutation studies to identify key residues in substrate and inhibitor binding.
Analysis of inhibition by various small molecule inhibitors and resistance to proteinaceous inhibitors.
Structural analysis of domain interactions influencing substrate access.

Main Results:

Carboxyl dyads in the C-terminal catalytic domain mediate substrate and inhibitor binding.
OB is efficiently inhibited by specific non-peptide inhibitors but not by large protein inhibitors.
The N-terminal beta-propeller domain restricts access for large substrates and inhibitors.

Conclusions:

Oligopeptidase B's unique catalytic activity and structural features present distinct biochemical properties.
Despite its unelucidated physiological role, OB is a significant virulence factor in animal trypanosomosis.
Its characteristics position Oligopeptidase B as a promising therapeutic target for drug development.