Cellulosome assembly: paradigms are meant to be broken!

Abstract:

:Cohesin-Dockerin interactions are at the core of cellulosomal assembly and organization. They are highly specific and form stable complexes, allowing cellulosomes to adopt distinct conformations. Each cellulosomal system seems to have a particular organizational strategy that can vary in complexity according to the nature of its Cohesin-Dockerin interactions. Hence, several efforts have been undertaken to reveal the mechanisms that govern the specificity, affinity and flexibility of these protein-protein interactions. Here we review the most recent studies that have focused on the structural aspects of Cohesin-Dockerin recognition. They reveal an ever-increasing number of subtle intricacies suggesting that cellulosome assembly is more complex than was initially thought.

journal_name

Curr Opin Struct Biol

authors

Bule P,Pires VM,Fontes CM,Alves VD

doi

10.1016/j.sbi.2018.03.012

subject

Has Abstract

pub_date

2018-04-01 00:00:00

pages

154-161

eissn

0959-440X

issn

1879-033X

pii

S0959-440X(17)30212-9

journal_volume

49

pub_type

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