5M2O

R. flavefaciens' third ScaB cohesin in complex with a group 1 dockerin

Summary for 5M2O

• Entry DOI: 10.2210/pdb5m2o/pdb
• Related: 5AOZ
• Descriptor: Putative cellulosomal scaffoldin protein, Group I Dockerin, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: cohesin, dockerin, complex, cellulosome, r. flavefaciens, structural protein, protein binding
• Biological source: Ruminococcus flavefaciens FD-1; More
• Total number of polymer chains: 2
• Total formula weight: 26316.41

Authors

Bule, P.,Najmudin, S.,Carvalho, A.L.,Fontes, C.M.G.A. (deposition date: 2016-10-13, release date: 2017-07-05, Last modification date: 2024-01-17)

Primary citation

Bule, P.,Alves, V.D.,Israeli-Ruimy, V.,Carvalho, A.L.,Ferreira, L.M.,Smith, S.P.,Gilbert, H.J.,Najmudin, S.,Bayer, E.A.,Fontes, C.M.
Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes.
Sci Rep, 7:759-759, 2017

PubMed Abstract: Cellulosomes are sophisticated multi-enzymatic nanomachines produced by anaerobes to effectively deconstruct plant structural carbohydrates. Cellulosome assembly involves the binding of enzyme-borne dockerins (Doc) to repeated cohesin (Coh) modules located in a non-catalytic scaffoldin. Docs appended to cellulosomal enzymes generally present two similar Coh-binding interfaces supporting a dual-binding mode, which may confer increased positional adjustment of the different complex components. Ruminococcus flavefaciens' cellulosome is assembled from a repertoire of 223 Doc-containing proteins classified into 6 groups. Recent studies revealed that Docs of groups 3 and 6 are recruited to the cellulosome via a single-binding mode mechanism with an adaptor scaffoldin. To investigate the extent to which the single-binding mode contributes to the assembly of R. flavefaciens cellulosome, the structures of two group 1 Docs bound to Cohs of primary (ScaA) and adaptor (ScaB) scaffoldins were solved. The data revealed that group 1 Docs display a conserved mechanism of Coh recognition involving a single-binding mode. Therefore, in contrast to all cellulosomes described to date, the assembly of R. flavefaciens cellulosome involves single but not dual-binding mode Docs. Thus, this work reveals a novel mechanism of cellulosome assembly and challenges the ubiquitous implication of the dual-binding mode in the acquisition of cellulosome flexibility.

PubMed: 28389644
DOI: 10.1038/s41598-017-00919-w

Experimental method

X-RAY DIFFRACTION (1.26 Å)