Publication
Article Metrics
Citations
Online attention
Assembly of Ruminococcus flavefaciens cellulosome revealed by structures of two cohesin-dockerin complexes
DOI:
10.1038/s41598-017-00919-w
Authors:
Pedro
Bule
(CIISA-Faculdade de Medicina Veterinária, Universidade de Lisboa)
,
Victor
Alves
(CIISA-Faculdade de Medicina Veterinária, Universidade de Lisboa)
,
Vered
Israeli-ruimy
(The Weizmann Institute of Science)
,
Ana Luisa
Carvalho
(UCIBIO-REQUIMTE)
,
Luís M. A.
Ferreira
(CIISA – Faculdade de Medicina Veterinária)
,
Steven P.
Smith
(Queen’s University)
,
Harry J.
Gilbert
(Newcastle University)
,
Shabir
Najmudin
(CIISA – Faculdade de Medicina Veterinária)
,
Edward A.
Bayer
(The Weizmann Institute of Science)
,
Carlos M. G. A.
Fontes
(CIISA – Faculdade de Medicina Veterinária)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Scientific Reports
, VOL 7
State:
Published (Approved)
Published:
April 2017
Diamond Proposal Number(s):
8425

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.
Journal Keywords: Bacteria; X-ray crystallography
Subject Areas:
Biology and Bio-materials
Instruments:
I04-1-Macromolecular Crystallography (fixed wavelength)
Other Facilities: European Synchrotron Radiation Facility (ESRF)
Documents:
art%3A10.1038%2Fs41598-017-00919-w.pdf
Discipline Tags:
Technical Tags: