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5K39

THE TYPE II COHESIN DOCKERIN COMPLEX FROM CLOSTRIDIUM THERMOCELLUM

Summary for 5K39
Entry DOI10.2210/pdb5k39/pdb
DescriptorCellulosome anchoring protein cohesin region, Dockerin module from a protein of unknown function, CALCIUM ION, ... (4 entities in total)
Functional Keywordss-layer, secreted, cell wall, membrane protein, structural protein
Biological sourceRuminiclostridium thermocellum 27405
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Total number of polymer chains2
Total formula weight37273.11
Authors
Viegas, A.,Pinheiro, B.,Bras, J.L.A.,Romao, M.J.,Alves, V.,Carvalho, A.L.,Fontes, C.M.G.A. (deposition date: 2016-05-19, release date: 2017-03-29, Last modification date: 2024-01-10)
Primary citationBras, J.L.,Pinheiro, B.A.,Cameron, K.,Cuskin, F.,Viegas, A.,Najmudin, S.,Bule, P.,Pires, V.M.,Romao, M.J.,Bayer, E.A.,Spencer, H.L.,Smith, S.,Gilbert, H.J.,Alves, V.D.,Carvalho, A.L.,Fontes, C.M.
Diverse specificity of cellulosome attachment to the bacterial cell surface.
Sci Rep, 6:38292-38292, 2016
Cited by
PubMed Abstract: During the course of evolution, the cellulosome, one of Nature's most intricate multi-enzyme complexes, has been continuously fine-tuned to efficiently deconstruct recalcitrant carbohydrates. To facilitate the uptake of released sugars, anaerobic bacteria use highly ordered protein-protein interactions to recruit these nanomachines to the cell surface. Dockerin modules located within a non-catalytic macromolecular scaffold, whose primary role is to assemble cellulosomal enzymatic subunits, bind cohesin modules of cell envelope proteins, thereby anchoring the cellulosome onto the bacterial cell. Here we have elucidated the unique molecular mechanisms used by anaerobic bacteria for cellulosome cellular attachment. The structure and biochemical analysis of five cohesin-dockerin complexes revealed that cell surface dockerins contain two cohesin-binding interfaces, which can present different or identical specificities. In contrast to the current static model, we propose that dockerins utilize multivalent modes of cohesin recognition to recruit cellulosomes to the cell surface, a mechanism that maximises substrate access while facilitating complex assembly.
PubMed: 27924829
DOI: 10.1038/srep38292
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.98 Å)
Structure validation

227344

數據於2024-11-13公開中

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