Differential contribution of tryptophans to the folding and stability of the attachment invasion locus transmembrane β-barrel from Yersinia pestis.

ABSTRACT: Attachment invasion locus (Ail) protein of Yersinia pestis is a crucial outer membrane protein for host invasion and determines bacterial survival within the host. Despite its importance in pathogenicity, surprisingly little is known on Ail biophysical properties. We investigate the contribution of micelle concentrations and interface tryptophans on the Ail β-barrel refolding and unfolding processes. Our results reveal that barrel folding is surprisingly independent of micelle amounts, but proceeds through an on-pathway intermediate that requires the interface W42 for cooperative barrel refolding. On the contrary, the unfolding event is strongly controlled by absolute micelle concentrations. We find that upon Trp → Phe substitution, protein stabilities follow the order W149F>WT>W42F for th

SUBMITTER: Gupta A 

PROVIDER: S-EPMC4179465 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature