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PDBsum entry 3pv0
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Transport protein, membrane protein
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PDB id
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3pv0
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Contents |
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370 a.a.
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483 a.a.
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282 a.a.
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370 a.a.
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PDB id:
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Transport protein, membrane protein
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Title:
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Crystal structure of a pre-translocation state mbp-maltose transporter complex without nucleotide
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Structure:
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Maltose transporter subunit. Periplasmic-binding component of abc superfamily. Chain: e. Fragment: unp residues 27-396. Engineered: yes. Maltose transporter subunit. Membrane component of abc superfamily. Chain: f. Engineered: yes.
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Source:
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Escherichia coli. Organism_taxid: 83333. Strain: k12. Gene: ecdh10b_4223, male. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ecdh10b_4222, malf. Gene: ecdh10b_4221, malg. Gene: ecdh10b_4224, malk.
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Resolution:
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3.10Å
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R-factor:
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0.233
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R-free:
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0.274
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Authors:
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M.L.Oldham,J.Chen
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Key ref:
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M.L.Oldham
and
J.Chen
(2011).
Crystal structure of the maltose transporter in a pretranslocation intermediate state.
Science,
332,
1202-1205.
PubMed id:
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Date:
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06-Dec-10
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Release date:
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18-May-11
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PROCHECK
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Headers
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References
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P0AEX9
(MALE_ECOLI) -
Maltose/maltodextrin-binding periplasmic protein from Escherichia coli (strain K12)
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Seq:
Struc:
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396 a.a.
370 a.a.*
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P02916
(MALF_ECOLI) -
Maltose/maltodextrin transport system permease protein MalF from Escherichia coli (strain K12)
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Seq:
Struc:
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514 a.a.
483 a.a.
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Enzyme class:
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Chains A, B:
E.C.7.5.2.1
- ABC-type maltose transporter.
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Reaction:
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D-maltose(out) + ATP + H2O = D-maltose(in) + ADP + phosphate + H+
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D-maltose(out)
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+
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ATP
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+
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H2O
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=
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D-maltose(in)
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+
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ADP
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+
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phosphate
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Science
332:1202-1205
(2011)
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PubMed id:
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Crystal structure of the maltose transporter in a pretranslocation intermediate state.
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M.L.Oldham,
J.Chen.
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ABSTRACT
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Adenosine triphosphate (ATP)-binding cassette (ABC) transporters convert
chemical energy from ATP hydrolysis to mechanical work for substrate
translocation. They function by alternating between two states, exposing the
substrate-binding site to either side of the membrane. A key question that
remains to be addressed is how substrates initiate the transport cycle. Using
x-ray crystallography, we have captured the maltose transporter in an
intermediate step between the inward- and outward-facing states. We show that
interactions with substrate-loaded maltose-binding protein in the periplasm
induce a partial closure of the MalK dimer in the cytoplasm. ATP binding to this
conformation then promotes progression to the outward-facing state. These
results, interpreted in light of biochemical and functional studies, provide a
structural basis to understand allosteric communication in ABC transporters.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.S.Woo,
A.Zeltina,
B.A.Goetz,
and
K.P.Locher
(2012).
X-ray structure of the Yersinia pestis heme transporter HmuUV.
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Nat Struct Mol Biol,
19,
1310-1315.
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PDB code:
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V.M.Korkhov,
S.A.Mireku,
and
K.P.Locher
(2012).
Structure of AMP-PNP-bound vitamin B12 transporter BtuCD-F.
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Nature,
490,
367-372.
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PDB code:
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V.van Noort,
J.Seebacher,
S.Bader,
S.Mohammed,
I.Vonkova,
M.J.Betts,
S.Kühner,
R.Kumar,
T.Maier,
M.O'Flaherty,
V.Rybin,
A.Schmeisky,
E.Yus,
J.Stülke,
L.Serrano,
R.B.Russell,
A.J.Heck,
P.Bork,
and
A.C.Gavin
(2012).
Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.
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Mol Syst Biol,
8,
571.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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