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PDBsum entry 4hzu
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Hydrolase, transport protein
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PDB id
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4hzu
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Contents |
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284 a.a.
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273 a.a.
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240 a.a.
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164 a.a.
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References listed in PDB file
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Key reference
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Title
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Structure of a bacterial energy-Coupling factor transporter.
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Authors
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T.Wang,
G.Fu,
X.Pan,
J.Wu,
X.Gong,
J.Wang,
Y.Shi.
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Ref.
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Nature, 2013,
497,
272-276.
[DOI no: ]
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PubMed id
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Abstract
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The energy-coupling factor (ECF) transporters constitute a novel family of
conserved membrane transporters in prokaryotes that have a similar domain
organization to the ATP-binding cassette transporters. Each ECF transporter
comprises a pair of cytosolic ATPases (the A and A' components, or EcfA and
EcfA'), a membrane-embedded substrate-binding protein (the S component, or EcfS)
and a transmembrane energy-coupling component (the T component, or EcfT) that
links the EcfA-EcfA' subcomplex to EcfS. The structure and transport mechanism
of the quaternary ECF transporter remain largely unknown. Here we report the
crystal structure of a nucleotide-free ECF transporter from Lactobacillus brevis
at a resolution of 3.5 Å. The T component has a horseshoe-shaped open
architecture, with five α-helices as transmembrane segments and two cytoplasmic
α-helices as coupling modules connecting to the A and A' components.
Strikingly, the S component, thought to be specific for hydroxymethyl
pyrimidine, lies horizontally along the lipid membrane and is bound exclusively
by the five transmembrane segments and the two cytoplasmic helices of the T
component. These structural features suggest a plausible working model for the
transport cycle of the ECF transporters.
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