Bacterial adhesins: structural studies reveal chaperone function and pilus biogenesis.

Abstract:

:During the past year, remarkable progress has been made in understanding how periplasmic chaperones fold and protect protein modules that are destined for assembly into adhesive pili in Gram-negative bacteria. The first two three-dimensional structures of complexes of periplasmic chaperones with substrate pilus subunits have revealed much about the structural basis for chaperone-mediated folding and aggregation prevention, and have provided insight into the structure of adhesive pili.

journal_name

Curr Opin Chem Biol

authors

Knight SD,Berglund J,Choudhury D

doi

10.1016/s1367-5931(00)00144-7

subject

Has Abstract

pub_date

2000-12-01 00:00:00

pages

653-60

issue

6

eissn

1367-5931

issn

1879-0402

pii

S1367-5931(00)00144-7

journal_volume

4

pub_type

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