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5M2S

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

Summary for 5M2S
Entry DOI10.2210/pdb5m2s/pdb
Related5AOZ 5M2O
DescriptorPutative cellulosomal scaffoldin protein, Doc8: Type I dockerin repeat domain from family 9 glycoside hydrolase WP_009982745[Ruminococcus flavefaciens], CALCIUM ION, ... (5 entities in total)
Functional Keywordscohesin, dockerin, complex, cellulosome, r. flavefaciens, cell adhesion, protein binding
Biological sourceRuminococcus flavefaciens
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Total number of polymer chains2
Total formula weight27302.31
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 citationBule, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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