Browse by author
Lookup NU author(s): Dr Alexandra Carvalho, Emeritus Professor Harry Gilbert
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
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 β-strands and a small α-helix. The β-strands assemble into two elongated β-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 β-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 β-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. © 2005 Published by Elsevier Ltd.
Author(s): Carvalho AL, Pires VMR, Gloster TM, Turkenburg JP, Prates JAM, Ferreira LMA, Romao MJ, Davies GJ, Fontes CMGA, Gilbert HJ
Publication type: Article
Publication status: Published
Journal: Journal of Molecular Biology
Year: 2005
Volume: 349
Issue: 5
Pages: 909-915
ISSN (print): 0022-2836
ISSN (electronic): 1089-8638
Publisher: Academic Press
URL: http://dx.doi.org/10.1016/j.jmb.2005.04.037
DOI: 10.1016/j.jmb.2005.04.037
PubMed id: 15913653
Altmetrics provided by Altmetric
