2bm3

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spinqualitylabelsall models 2bm3, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

STRUCTURE OF THE TYPE II COHESIN FROM CLOSTRIDIUM THERMOCELLUM SDBA

Overview

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, alpha-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.

About this Structure

2BM3 is a Single protein structure of sequence from Clostridium thermocellum with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Insights into the structural determinants of cohesin-dockerin specificity revealed by the crystal structure of the type II cohesin from Clostridium thermocellum SdbA., Carvalho AL, Pires VM, Gloster TM, Turkenburg JP, Prates JA, Ferreira LM, Romao MJ, Davies GJ, Fontes CM, Gilbert HJ, J Mol Biol. 2005 Jun 24;349(5):909-15. PMID:15913653

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