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Contents |
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* Residue conservation analysis
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Enzyme class:
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Chains C, D:
E.C.7.6.2.8
- ABC-type vitamin B12 transporter.
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Reaction:
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an R-cob(III)alamin(out) + ATP + H2O = an R-cob(III)alamin(in) + ADP + phosphate + H+
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R-cob(III)alamin(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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R-cob(III)alamin(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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DOI no:
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Science
296:1091-1098
(2002)
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PubMed id:
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The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism.
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K.P.Locher,
A.T.Lee,
D.C.Rees.
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ABSTRACT
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The ABC transporters are ubiquitous membrane proteins that couple adenosine
triphosphate (ATP) hydrolysis to the translocation of diverse substrates across
cell membranes. Clinically relevant examples are associated with cystic fibrosis
and with multidrug resistance of pathogenic bacteria and cancer cells. Here, we
report the crystal structure at 3.2 angstrom resolution of the Escherichia coli
BtuCD protein, an ABC transporter mediating vitamin B12 uptake. The two
ATP-binding cassettes (BtuD) are in close contact with each other, as are the
two membrane-spanning subunits (BtuC); this arrangement is distinct from that
observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20
transmembrane helices grouped around a translocation pathway that is closed to
the cytoplasm by a gate region whereas the dimer arrangement of the BtuD
subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A
prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding
cassette and appears to represent a conserved motif among the ABC transporters.
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Selected figure(s)
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Figure 4.
Fig. 4. Transport pathway for B[12] through the BtuCD
transporter. The backbone of the B[12] transporter is shown in a
side view, with the four subunits colored as in Fig. 3A. The
cavity at the interface between the two membrane-spanning BtuC
subunits is shown as a semi-transparent, yellow surface and was
calculated with a probe radius of 2 Å using the program
MSMS (59). The B[12] molecule shown in CPK was manually docked
into the cavity and is not present in the structure. The gate
region is shown in light blue.
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Figure 7.
Fig. 7. Schematic mechanism of vitamin B[12] import through the
BtuCD transporter. The membrane-spanning and ABC cassette
subunits are depicted as C and D, respectively, and the
periplasmic binding protein BtuF as F. The gray ribbon
represents the cytoplasmic membrane. On the left, the
nucleotide-free state of the transporter is shown. On the right,
proposed rearrangements during translocation of vitamin B[12]
are depicted. See text for further explanation.
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The above figures are
reprinted
by permission from the AAAs:
Science
(2002,
296,
1091-1098)
copyright 2002.
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Figures were
selected
by an automated process.
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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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| |
Nat Struct Mol Biol,
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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,
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PDB code:
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A.S.Oliveira,
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PDB code:
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Fungal Genet Biol,
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(2010).
Identification and modeling of a drug target for Clostridium perfringens SM101.
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Bioinformation,
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H.Shimizu,
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K.Kono,
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A stable ATP binding to the nucleotide binding domain is important for reliable gating cycle in an ABC transporter CFTR.
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FEBS J,
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J Biol Chem,
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Anal Bioanal Chem,
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K.McLuskey,
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Eur Biophys J,
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K.Okuda,
S.Yanagihara,
T.Sugayama,
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J.Nakayama,
and
K.Sonomoto
(2010).
Functional significance of the E loop, a novel motif conserved in the lantibiotic immunity ATP-binding cassette transport systems.
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J Bacteriol,
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(2010).
A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation.
|
| |
Nat Struct Mol Biol,
17,
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|
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|
|
S.Atwell,
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H.A.Lewis,
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| |
Protein Eng Des Sel,
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PDB codes:
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S.Igarashi,
M.Osawa,
S.Ozawa,
and
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(2010).
Backbone resonance assignments for the ligand binding subunit of the histidine permease complex (HisJ) from Escherichia coli, under histidine-bound and unbound states.
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| |
Biomol NMR Assign,
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(2010).
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(2010).
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J Gen Physiol,
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C.Schölz,
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Alternating access in maltose transporter mediated by rigid-body rotations.
|
| |
Mol Cell,
33,
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|
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PDB code:
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D.Muallem,
and
P.Vergani
(2009).
Review. ATP hydrolysis-driven gating in cystic fibrosis transmembrane conductance regulator.
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Solute-binding sites in ABC transporters for recognition, occlusion and trans-inhibition.
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ChemMedChem,
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E.Procko,
and
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(2009).
Antigen processing and presentation: TAPping into ABC transporters.
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| |
Curr Opin Immunol,
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Molecular models of human P-glycoprotein in two different catalytic states.
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BMC Struct Biol,
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J.Ma,
K.Fan,
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Asymmetric conformational flexibility in the ATP-binding cassette transporter HI1470/1.
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Biophys J,
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N.Sumi,
R.Nagai,
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S.Kitaoka,
Y.Minami,
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Y.Takahashi,
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K.Fukuyama
(2009).
Molecular dynamism of Fe-S cluster biosynthesis implicated by the structure of the SufC(2)-SufD(2) complex.
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J Mol Biol,
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PDB code:
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L.R.Forrest,
and
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(2009).
The rocking bundle: a mechanism for ion-coupled solute flux by symmetrical transporters.
|
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Physiology (Bethesda),
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|
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M.A.Do Cao,
S.Crouzy,
M.Kim,
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D.S.Cafiso,
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Protein Sci,
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(2009).
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V.N.Bavro,
A.Welch,
T.A.Schaedler,
M.A.Seeger,
R.N.Miguel,
V.M.Korkhov,
H.W.van Veen,
H.Venter,
A.R.Walmsley,
C.G.Tate,
and
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Mass spectrometry of membrane transporters reveals subunit stoichiometry and interactions.
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| |
Nat Methods,
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|
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P.M.Jones,
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| |
Proteins,
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|
P.M.Jones,
M.L.O'Mara,
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P.Zou,
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Science,
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PDB codes:
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Mol Microbiol,
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S.Lukman,
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A network of dynamically conserved residues deciphers the motions of maltose transporter.
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| |
Proteins,
76,
588-597.
|
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|
S.Y.Huang,
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H.Y.Liu,
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(2009).
Molecular modeling of the heterodimer of human CFTR's nucleotide-binding domains using a protein-protein docking approach.
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| |
J Mol Graph Model,
27,
822-828.
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U.A.Hellmich,
and
C.Glaubitz
(2009).
NMR and EPR studies of membrane transporters.
|
| |
Biol Chem,
390,
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V.Kos,
and
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(2009).
The ATP-binding cassette family: a structural perspective.
|
| |
Cell Mol Life Sci,
66,
3111-3126.
|
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|
Y.X.Hou,
C.Z.Li,
K.Palaniyandi,
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L.Homolya,
B.Sarkadi,
and
X.B.Chang
(2009).
Effects of putative catalytic base mutation E211Q on ABCG2-mediated methotrexate transport.
|
| |
Biochemistry,
48,
9122-9131.
|
|
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Z.Ma,
F.E.Jacobsen,
and
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(2009).
Coordination chemistry of bacterial metal transport and sensing.
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Chem Rev,
109,
4644-4681.
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A.Ivetac,
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(2008).
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| |
Eur Biophys J,
37,
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A.J.Robinson,
C.Overy,
and
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(2008).
The mechanism of transport by mitochondrial carriers based on analysis of symmetry.
|
| |
Proc Natl Acad Sci U S A,
105,
17766-17771.
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A.L.Davidson,
E.Dassa,
C.Orelle,
and
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(2008).
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The membrane-associated lipoprotein-9 GmpC from Staphylococcus aureus binds the dipeptide GlyMet via side chain interactions.
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Biochemistry,
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PDB code:
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A.N.Antoniou,
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Assembly and export of MHC class I peptide ligands.
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Substrate-induced transmembrane signaling in the cobalamin transporter BtuB.
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Nat Struct Biol,
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PDB codes:
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D.Yernool,
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Biochemistry,
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On the role of the two extracytoplasmic substrate-binding domains in the ABC transporter OpuA.
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The distinct nucleotide binding states of the transporter associated with antigen processing (TAP) are regulated by the nonhomologous C-terminal tails of TAP1 and TAP2.
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Eur J Biochem,
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CFTR directly mediates nucleotide-regulated glutathione flux.
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EMBO J,
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Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer.
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EMBO J,
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J Bacteriol,
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A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle.
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Mol Cell,
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PDB codes:
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J.D.Campbell,
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and
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Potassium channel regulation.
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EMBO Rep,
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J.D.Campbell,
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Extending the structure of an ABC transporter to atomic resolution: modeling and simulation studies of MsbA.
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Biochemistry,
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J.D.Faraldo-Gómez,
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Acquisition of siderophores in gram-negative bacteria.
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Nat Rev Mol Cell Biol,
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The cobY gene of the archaeon Halobacterium sp. strain NRC-1 is required for de novo cobamide synthesis.
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J Bacteriol,
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MinD and role of the deviant Walker A motif, dimerization and membrane binding in oscillation.
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The making of the mitotic chromosome: modern insights into classical questions.
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Mol Cell,
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The structure and function of drug pumps: an update.
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Trends Microbiol,
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N-terminal transmembrane domain of the SUR controls trafficking and gating of Kir6 channel subunits.
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Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers.
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Proc Natl Acad Sci U S A,
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Effect of detergents on the association of the glycophorin a transmembrane helix.
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The alternating ATPase domains of MutS control DNA mismatch repair.
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EMBO J,
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PDB code:
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Three-dimensional crystallization of the Escherichia coli glycerol-3-phosphate transporter: a member of the major facilitator superfamily.
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Protein Sci,
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ATP hydrolysis is required for cohesin's association with chromosomes.
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On the mechanism of MgATP-dependent gating of CFTR Cl- channels.
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J Gen Physiol,
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Parasite plastids: maintenance and functions.
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Philos Trans R Soc Lond B Biol Sci,
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Multidrug-exporting secondary transporters.
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Acta Crystallogr D Biol Crystallogr,
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K.Diederichs,
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W.Boos,
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Crystallization and preliminary X-ray analysis of the trehalose/maltose ABC transporter MalFGK2 from Thermococcus litoralis.
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Acta Crystallogr D Biol Crystallogr,
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Identification of the gene responsible for the cblA complementation group of vitamin B12-responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements.
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Proc Natl Acad Sci U S A,
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Vanadate-catalyzed photocleavage of the signature motif of an ATP-binding cassette (ABC) transporter.
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Proc Natl Acad Sci U S A,
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The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter.
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Proc Natl Acad Sci U S A,
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PDB code:
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How are the ABC transporters energized?
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Proc Natl Acad Sci U S A,
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ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer.
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Mol Cell,
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PDB code:
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P.M.Jones,
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Crystal structure of bacterial multidrug efflux transporter AcrB.
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Nature,
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PDB code:
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|
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|
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|
S.Rouhani,
M.T.Facciotti,
G.Woodcock,
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The membrane protein FeoB contains an intramolecular G protein essential for Fe(II) uptake in bacteria.
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Proc Natl Acad Sci U S A,
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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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