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Crystal and solution structures of a prokaryotic m16b peptidase: An open and shut case

Academic Article
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Overview

authors

  • Aleshin, A. E.
  • Gramatikova, S.
  • Hura, G. L.
  • Bobkov, A.
  • Strongin, A. Y.
  • Stec, B.
  • Tainer, John
  • Liddington, R. C.
  • Smith, J. W.

publication date

  • November 2009

journal

  • Structure  Journal

abstract

  • The M16 family of zinc peptidases comprises a pair of homologous domains that form two halves of a "clam-shell" surrounding the active site. The M16A and M16C subfamilies form one class ("peptidasomes"): they degrade 30-70 residue peptides, and adopt both open and closed conformations. The eukaryotic M16B subfamily forms a second class ("processing proteases"): they adopt a single partly-open conformation that enables them to cleave signal sequences from larger proteins. Here, we report the solution and crystal structures of a prokaryotic M16B peptidase, and demonstrate that it has features of both classes: thus, it forms stable "open" homodimers in solution that resemble the processing proteases; but the clam-shell closes upon binding substrate, a feature of the M16A/C peptidasomes. Moreover, clam-shell closure is required for proteolytic activity. We predict that other prokaryotic M16B family members will form dimeric peptidasomes, and propose a model for the evolution of the M16 family.

subject areas

  • Amino Acid Sequence
  • Bacillus
  • Bacterial Proteins
  • Base Sequence
  • Computational Biology
  • Crystallography
  • Dimerization
  • Metalloendopeptidases
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Sequence Alignment
  • Zinc
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Identity

PubMed Central ID

  • PMC3615642

International Standard Serial Number (ISSN)

  • 0969-2126

Digital Object Identifier (DOI)

  • 10.1016/j.str.2009.09.009

PubMed ID

  • 19913481
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Additional Document Info

start page

  • 1465

end page

  • 1475

volume

  • 17

issue

  • 11

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