2bm3
From Proteopedia
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==Overview== | ==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 .. | + | 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== | ==About this Structure== | ||
| - | 2BM3 is a | + | 2BM3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum] with IPA as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BM3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: type 2]] | [[Category: type 2]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:44:11 2007'' |
Revision as of 11:38, 5 November 2007
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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 IPA as ligand. Structure known Active Site: AC1. 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
Page seeded by OCA on Mon Nov 5 13:44:11 2007
Categories: Clostridium thermocellum | Single protein | Carvalho, A.L. | Davies, G.J. | Ferreira, L.M.A. | Fontes, C.M.G.A. | Gilbert, H.J. | Gloster, T.M. | Pires, V.M.R. | Prates, J.A.M. | Proctor, M.R. | Romao, M.J. | Turkenburg, J.P. | IPA | Cellulosome | Cohesin | Dockerin | Nuclear protein | Type 2
