3UL4

Crystal structure of Coh-OlpA(Cthe_3080)-Doc918(Cthe_0918) complex: A novel type I Cohesin-Dockerin complex from Clostridium thermocellum ATTC 27405

3UL4 の概要

• エントリーDOI: 10.2210/pdb3ul4/pdb
• 分子名称: Cellulosome-anchoring protein, Cellulosome enzyme, dockerin type I, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: cellulosome, cohesin, dockerin, type i cohesin-dockerin complex, protein-protein interaction, clostridium thermocellum, cell adhesion, cell adhesion-protein binding complex, cell adhesion/protein binding
• 由来する生物種: Clostridium thermocellum; 詳細
• 細胞内の位置: Secreted, cell wall, S-layer: Q06848
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25632.22

構造登録者

Alves, V.D.,Carvalho, A.L.,Najmudin, S.H.,Bras, J.,Prates, J.A.M.,Fontes, C.M.G.A. (登録日: 2011-11-10, 公開日: 2012-11-28, 最終更新日: 2024-02-28)

主引用文献

Bras, J.L.,Alves, V.D.,Carvalho, A.L.,Najmudin, S.,Prates, J.A.,Ferreira, L.M.,Bolam, D.N.,Romao, M.J.,Gilbert, H.J.,Fontes, C.M.
Novel Clostridium thermocellum Type I Cohesin-Dockerin Complexes Reveal a Single Binding Mode.
J.Biol.Chem., 287:44394-44405, 2012

PubMed Abstract: Protein-protein interactions play a pivotal role in a large number of biological processes exemplified by the assembly of the cellulosome. Integration of cellulosomal components occurs through the binding of type I cohesin modules located in a non-catalytic molecular scaffold to type I dockerin modules located at the C terminus of cellulosomal enzymes. The majority of type I dockerins display internal symmetry reflected by the presence of two essentially identical cohesin-binding surfaces. Here we report the crystal structures of two novel Clostridium thermocellum type I cohesin-dockerin complexes (CohOlpC-Doc124A and CohOlpA-Doc918). The data revealed that the two dockerins, Doc918 and Doc124A, are unusual because they lack the structural symmetry required to support a dual binding mode. Thus, in both cases, cohesin recognition is dominated by residues located at positions 11, 12, and 19 of one of the dockerin binding surfaces. The alternative binding mode is not possible (Doc918) or highly limited (Doc124A) because residues that assume the critical interacting positions, when dockerins are reoriented by 180°, make steric clashes with the cohesin. In common with a third dockerin (Doc258) that also presents a single binding mode, Doc124A directs the appended cellulase, Cel124A, to the surface of C. thermocellum and not to cellulosomes because it binds preferentially to type I cohesins located at the cell envelope. Although there are a few exceptions, such as Doc918 described here, these data suggest that there is considerable selective pressure for the evolution of a dual binding mode in type I dockerins that direct enzymes into cellulosomes.

PubMed: 23118225
DOI: 10.1074/jbc.M112.407700

実験手法

X-RAY DIFFRACTION (1.95 Å)