@article {11024,
	title = {Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes},
	journal = {Scientific Reports},
	volume = {7},
	year = {2017},
	note = {<p>n/a</p>
},
	month = {2017},
	pages = {759},
	abstract = {<p>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{\textquoteright} 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.</p>
},
	isbn = {2045-2322},
	url = {http://dx.doi.org/10.1038/s41598-017-00919-w},
	author = {Bule, Pedro and Alves, Victor D. and Israeli-Ruimy, Vered and Carvalho, Ana L. and Ferreira, Lu{\'\i}s M. A. and Smith, Steven P. and Gilbert, Harry J. and Najmudin, Shabir and Bayer, Edward A. and Fontes, Carlos M. G. A.}
}
