Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD.

Abstract:

:SlyD is a bacterial two-domain protein that functions as a molecular chaperone, a prolyl cis/trans isomerase, and a nickel-binding protein. This review summarizes recent findings about the molecular enzyme mechanism of SlyD. The chaperone function located in one domain of SlyD is involved in twin-arginine translocation and increases the catalytic efficiency of the prolyl cis/trans isomerase domain in protein folding by two orders of magnitude. The C-terminal tail of SlyD binds Ni2+ ions and supplies them for the maturation of [NiFe] hydrogenases. A combined biochemical and biophysical analysis revealed the molecular basis of the delicate interplay of the different domains of SlyD for optimal function.

journal_name

Biol Chem

journal_title

Biological chemistry

authors

Kovermann M,Schmid FX,Balbach J

doi

10.1515/hsz-2013-0137

subject

Has Abstract

pub_date

2013-08-01 00:00:00

pages

965-75

issue

8

eissn

1431-6730

issn

1437-4315

pii

/j/bchm.just-accepted/hsz-2013-0137/hsz-2013-0137.

journal_volume

394

pub_type

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