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PDBsum entry 2kfw
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References listed in PDB file
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Key reference
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Title
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The interaction of the escherichia coli protein slyd with nickel ions illuminates the mechanism of regulation of its peptidyl-Prolyl isomerase activity.
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Authors
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L.Martino,
Y.He,
K.L.Hands-Taylor,
E.R.Valentine,
G.Kelly,
C.Giancola,
M.R.Conte.
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Ref.
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Febs J, 2009,
276,
4529-4544.
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PubMed id
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Abstract
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The sensitive to lysis D (SlyD) protein from Escherichia coli is related to the
FK506-binding protein family, and it harbours both peptidyl-prolyl cis-trans
isomerase (PPIase) and chaperone-like activity, preventing aggregation and
promoting the correct folding of other proteins. Whereas a functional role of
SlyD as a protein-folding catalyst in vivo remains unclear, SlyD has been shown
to be an essential component for [Ni-Fe]-hydrogenase metallocentre assembly in
bacteria. Interestingly, the isomerase activity of SlyD is uniquely modulated by
nickel ions, which possibly regulate its functions in response to external
stimuli. In this work, we investigated the solution structure of SlyD and its
interaction with nickel ions, enabling us to gain insights into the molecular
mechanism of this regulation. We have revealed that the PPIase module of SlyD
contains an additional C-terminal alpha-helix packed against the catalytic site
of the domain; unexpectedly, our results show that the interaction of SlyD with
nickel ions entails participation of the novel structural features of the PPIase
domain, eliciting structural alterations of the catalytic pocket. We suggest
that such conformational rearrangements upon metal binding underlie the ability
of nickel ions to regulate the isomerase activity of SlyD.
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