The crystal structure of the MPN domain from the COP9 signalosome subunit CSN6

FEBS Lett. 2012 Apr 24;586(8):1147-53. doi: 10.1016/j.febslet.2012.03.029. Epub 2012 Mar 23.

Abstract

The COP9 signalosome (CSN) is a multiprotein complex containing eight subunits and is highly conserved from fungi to human. CSN is proposed to widely participate in many physiological processes, including protein degradation, DNA damage response and signal transduction. Among those subunits, only CSN5 and CSN6 belong to JAMM family. CSN5 possesses isopeptidase activity, but CSN6 lacks this ability. Here we report the 2.5Å crystal structure of MPN domain from Drosophila melanogaster CSN6. Structural comparison with other MPN domains, along with bioinformation analysis, suggests that MPN domain from CSN6 may serve as a scaffold instead of a metalloprotease.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • COP9 Signalosome Complex
  • Crystallography, X-Ray
  • Drosophila Proteins / chemistry*
  • Drosophila Proteins / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Multiprotein Complexes / chemistry*
  • Multiprotein Complexes / metabolism
  • Peptide Hydrolases / chemistry*
  • Peptide Hydrolases / metabolism
  • Protein Conformation
  • Protein Subunits / chemistry
  • Protein Subunits / metabolism

Substances

  • CSN6 protein, Drosophila
  • Drosophila Proteins
  • Multiprotein Complexes
  • Protein Subunits
  • Peptide Hydrolases
  • COP9 Signalosome Complex

Associated data

  • PDB/4E0Q