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PDBsum entry 3fvq
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References listed in PDB file
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Key reference
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Title
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Insights into how nucleotide-Binding domains power abc transport.
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Authors
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S.Newstead,
P.W.Fowler,
P.Bilton,
E.P.Carpenter,
P.J.Sadler,
D.J.Campopiano,
M.S.Sansom,
S.Iwata.
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Ref.
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Structure, 2009,
17,
1213-1222.
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PubMed id
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Abstract
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The mechanism by which nucleotide-binding domains (NBDs) of ABC transporters
power the transport of substrates across cell membranes is currently unclear.
Here we report the crystal structure of an NBD, FbpC, from the Neisseria
gonorrhoeae ferric iron uptake transporter with an unusual and substantial
domain swap in the C-terminal regulatory domain. This entanglement suggests that
FbpC is unable to open to the same extent as the homologous protein MalK. Using
molecular dynamics we demonstrate that this is not the case: both NBDs open
rapidly once ATP is removed. We conclude from this result that the closed
structures of FbpC and MalK have higher free energies than their respective open
states. This result has important implications for our understanding of the
mechanism of power generation in ABC transporters, because the unwinding of this
free energy ensures that the opening of these two NBDs is also powered.
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