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 Chemjournal_title
Biological chemistryauthors
Kovermann M,Schmid FX,Balbach Jdoi
10.1515/hsz-2013-0137subject
Has Abstractpub_date
2013-08-01 00:00:00pages
965-75issue
8eissn
1431-6730issn
1437-4315pii
/j/bchm.just-accepted/hsz-2013-0137/hsz-2013-0137.journal_volume
394pub_type
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