Insights into the structural determinants of cohesin dockerin specificity revealed by the crystal structure of the type II cohesin from Clostridium thermocellum SdbA

A L Carvalho, V M R Pires, T M Gloster, J P Turkenburg, J A M Prates, L M A Ferreira, M J Romao, G J Davies, C M G A Fontes, H J Gilbert

Research output: Contribution to journalArticlepeer-review

31 Citations (Scopus)

Abstract

The plant cell wall degrading enzymes expressed by anaerobic microorganisms form large multienzyme complexes (cellulosomes). Cellulosomes assemble by the Type I dockerins on the catalytic subunits binding to the reiterated Type I cohesins in the molecular scaffold, while Type II dockerin-cohesin interactions anchor the complex onto the bacterial cell surface. Type I and Type II cohesin, dockerin pairs show no cross-specificity. Here we report the crystal structure of the Type II cohesin (CohII) from the Clostridium thermocellum cell surface anchoring protein SdbA. The protein domain contains nine beta-strands and a small a-helix. The beta-strands assemble into two elongated beta-sheets that display a typical jelly roll fold. The structure of CohII is very similar to Type I cohesins, and the dockerin binding site, which is centred at beta-strands 3, 5 and 6, is likely to be conserved in the two proteins. Subtle differences in the topology of the binding sites and a lack of sequence identity in the beta-strands that comprise the core of the dockerin binding site explain why Type I and Type II cohesins display such distinct specificities for their target dockerins. (c) 2005 Published by Elsevier Ltd.

Original languageEnglish
Pages (from-to)909-915
Number of pages7
JournalJournal of Molecular Biology
Volume349
Issue number5
DOIs
Publication statusPublished - 24 Jun 2005

Keywords

  • cohesin
  • dockerin
  • cellulosome
  • cell-attachment
  • plant cell wall
  • PROTEIN CIPA
  • CELLULOSOME
  • DOMAIN
  • RECOGNITION
  • MODULE
  • CELLULOLYTICUM
  • SCAFFOLDIN
  • PROVIDES
  • COMPLEX
  • ENZYMES

Fingerprint

Dive into the research topics of 'Insights into the structural determinants of cohesin dockerin specificity revealed by the crystal structure of the type II cohesin from Clostridium thermocellum SdbA'. Together they form a unique fingerprint.

Cite this