5G5D

Crystal Structure of the CohScaC2-XDocCipA type II complex from Clostridium thermocellum

5G5D の概要

• エントリーDOI: 10.2210/pdb5g5d/pdb
• 分子名称: CELLULOSOME ANCHORING PROTEIN COHESIN REGION, CELLULOSOMAL-SCAFFOLDING PROTEIN A, CALCIUM ION (3 entities in total)
• 機能のキーワード: carbohydrate binding protein, cohesin-dockerin complex, type ii interaction, scaffoldin, cellulosome, c. thermocellum
• 由来する生物種: RUMINICLOSTRIDIUM THERMOCELLUM AD2; 詳細
• 細胞内の位置: Secreted: Q06851
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36806.85

構造登録者

Carvalho, A.L.,A Bras, J.L.,Najmudin, S.H.,Pinheiro, B.A.,Fontes, C.M.G.A. (登録日: 2016-05-23, 公開日: 2017-04-05, 最終更新日: 2024-01-10)

主引用文献

Bras, 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

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

実験手法

X-RAY DIFFRACTION (3 Å)