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PDBsum entry 2fcp
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Membrane protein
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PDB id
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2fcp
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Contents |
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* Residue conservation analysis
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DOI no:
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Science
282:2215-2220
(1998)
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PubMed id:
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Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide.
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A.D.Ferguson,
E.Hofmann,
J.W.Coulton,
K.Diederichs,
W.Welte.
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ABSTRACT
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FhuA, the receptor for ferrichrome-iron in Escherichia coli, is a member of a
family of integral outer membrane proteins, which, together with the
energy-transducing protein TonB, mediate the active transport of ferric
siderophores across the outer membrane of Gram-negative bacteria. The
three-dimensional structure of FhuA is presented here in two conformations: with
and without ferrichrome-iron at resolutions of 2.7 and 2.5 angstroms,
respectively. FhuA is a beta barrel composed of 22 antiparallel beta strands. In
contrast to the typical trimeric arrangement found in porins, FhuA is monomeric.
Located within the beta barrel is a structurally distinct domain, the
"cork," which mainly consists of a four-stranded beta sheet and four
short alpha helices. A single lipopolysaccharide molecule is noncovalently
associated with the membrane-embedded region of the protein. Upon binding of
ferrichrome-iron, conformational changes are transduced to the periplasmic
pocket of FhuA, signaling the ligand-loaded status of the receptor. Sequence
homologies and mutagenesis data are used to propose a structural mechanism for
TonB-dependent siderophore-mediated transport across the outer membrane.
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Selected figure(s)
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Figure 3.
Fig. 3. Representative section of the electron density map.
Stereoview of the final 3F[obs]-2F[calc] electron density map
(blue) at a resolution of 2.7 Å is contoured at 1.5  , showing
the ferrichrome-iron binding site, including water molecules.
The ferrichrome-iron molecule is shown in yellow, and the iron
atom is indicated as a large red sphere. Select side-chain
residues (Glu98, Gly99, and Gln100 from apex B; Tyr116 from apex
C; Tyr244 and Trp246 from L3; Phe^313 from  7; Phe^391
from 9; and
Phe^702 from 21) and the
two water molecules (Wat151 and Wat154) found in the binding
site are labeled (34) and colored white and red, respectively.
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Figure 4.
Fig. 4. Conformational changes induced upon ferrichrome-iron
binding. Superposition of the  -carbon
coordinates of FhuA and its complex with ferrichrome-iron
illustrating the ligand-induced conformational changes observed
in the cork domain. The cork domains of FhuA and its complex
with ferrichrome-iron are shown in purple and yellow,
respectively. The barrel strands (shown in blue) are represented
as thin lines for clarity of the cork domain. Apices A, B, and C
and Glu19 are labeled (34).
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The above figures are
reprinted
by permission from the AAAs:
Science
(1998,
282,
2215-2220)
copyright 1998.
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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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C.T.Lin,
C.C.Wu,
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Fur regulation of the capsular polysaccharide biosynthesis and iron-acquisition systems in Klebsiella pneumoniae CG43.
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Microbiology,
157,
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K.D.Krewulak,
and
H.J.Vogel
(2011).
TonB or not TonB: is that the question?
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Biochem Cell Biol,
89,
87-97.
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N.Muhammad,
T.Dworeck,
M.Fioroni,
and
U.Schwaneberg
(2011).
Engineering of the E. coli Outer Membrane Protein FhuA to overcome the Hydrophobic Mismatch in Thick Polymeric Membranes.
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J Nanobiotechnology,
9,
8.
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V.Karuppiah,
J.L.Berry,
and
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Outer membrane translocons: structural insights into channel formation.
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Trends Microbiol,
19,
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A.Güven,
M.Fioroni,
B.Hauer,
and
U.Schwaneberg
(2010).
Molecular understanding of sterically controlled compound release through an engineered channel protein (FhuA).
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J Nanobiotechnology,
8,
14.
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A.J.Beddek,
and
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Biometals,
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Eur Biophys J,
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An active site water network in the plasminogen activator pla from Yersinia pestis.
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Structure,
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PDB codes:
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K.R.Vinothkumar,
and
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Temperature-induced changes in the lipopolysaccharide of Yersinia pestis affect plasminogen activation by the pla surface protease.
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Infect Immun,
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N.Noinaj,
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TonB-dependent transporters: regulation, structure, and function.
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Annu Rev Microbiol,
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R.C.Hider,
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Chemistry and biology of siderophores.
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S.D.Köhler,
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W.Welte,
and
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The proline-rich domain of TonB possesses an extended polyproline II-like conformation of sufficient length to span the periplasm of Gram-negative bacteria.
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Protein Sci,
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S.S.Chng,
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Proc Natl Acad Sci U S A,
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Immunization with the Haemophilus ducreyi hemoglobin receptor HgbA with adjuvant monophosphoryl lipid A protects swine from a homologous but not a heterologous challenge.
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Infect Immun,
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A.Bhunia,
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J Biol Chem,
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A.Bhunia,
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Biopolymers,
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C.A.Kors,
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Effects of impurities on membrane-protein crystallization in different systems.
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Acta Crystallogr D Biol Crystallogr,
65,
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C.R.Smallwood,
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Q.Xiao,
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and
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Reconstitution of bacterial outer membrane TonB-dependent transporters in planar lipid bilayer membranes.
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Proc Natl Acad Sci U S A,
106,
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I.J.Schalk,
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and
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Structure-function relationships in the bifunctional ferrisiderophore FpvA receptor from Pseudomonas aeruginosa.
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J.Mares,
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and
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284,
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and
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Acta Crystallogr D Biol Crystallogr,
65,
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PDB code:
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L.Rutten,
J.P.Mannie,
C.M.Stead,
C.R.Raetz,
C.M.Reynolds,
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M.R.Egmond,
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and
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Active-site architecture and catalytic mechanism of the lipid A deacylase LpxR of Salmonella typhimurium.
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Proc Natl Acad Sci U S A,
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PDB code:
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M.Sandy,
and
A.Butler
(2009).
Microbial iron acquisition: marine and terrestrial siderophores.
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Chem Rev,
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S.Krieg,
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P.Delepelaire,
and
W.Welte
(2009).
Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex.
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Proc Natl Acad Sci U S A,
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PDB codes:
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S.Raunser,
and
T.Walz
(2009).
Electron crystallography as a technique to study the structure on membrane proteins in a lipidic environment.
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Mol Cell,
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PDB codes:
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T.H.Yun,
J.E.Cott,
R.I.Tapping,
J.M.Slauch,
and
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Proteolytic inactivation of tissue factor pathway inhibitor by bacterial omptins.
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Blood,
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T.H.Yun,
and
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Polyphosphate and omptins: novel bacterial procoagulant agents.
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J Cell Mol Med,
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V.Braun
(2009).
FhuA (TonA), the career of a protein.
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J Bacteriol,
191,
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H.Boze,
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A.Padilla,
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and
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NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: Model of the possible lipid A-binding site.
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Biopolymers,
91,
207-220.
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PDB code:
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Z.Ma,
F.E.Jacobsen,
and
D.P.Giedroc
(2009).
Coordination chemistry of bacterial metal transport and sensing.
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Chem Rev,
109,
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A.L.Davidson,
E.Dassa,
C.Orelle,
and
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Structure, function, and evolution of bacterial ATP-binding cassette systems.
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Microbiol Mol Biol Rev,
72,
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and
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Signaling mechanisms for activation of extracytoplasmic function (ECF) sigma factors.
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Biochim Biophys Acta,
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M.D.Rigden,
and
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Expression, purification, and structural characterization of CfrA, a putative iron transporter from Campylobacter jejuni.
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J Bacteriol,
190,
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C.N.Cornelissen
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Identification and characterization of gonococcal iron transport systems as potential vaccine antigens.
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Future Microbiol,
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Interaction of chitosans and their N-acylated derivatives with lipopolysaccharide of gram-negative bacteria.
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Biochemistry (Mosc),
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H.Remaut,
C.Tang,
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D.G.Thanassi,
G.Waksman,
and
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(2008).
Fiber formation across the bacterial outer membrane by the chaperone/usher pathway.
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Cell,
133,
640-652.
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PDB code:
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J.M.Noto,
and
C.N.Cornelissen
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Identification of TbpA residues required for transferrin-iron utilization by Neisseria gonorrhoeae.
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Infect Immun,
76,
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K.J.James,
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F.Molina,
and
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TonB induces conformational changes in surface-exposed loops of FhuA, outer membrane receptor of Escherichia coli.
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Protein Sci,
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K.Zeth,
C.Römer,
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Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli.
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J Biol Chem,
283,
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PDB codes:
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R.Shi,
M.Pineda,
E.Ajamian,
Q.Cui,
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Structure of L-xylulose-5-Phosphate 3-epimerase (UlaE) from the anaerobic L-ascorbate utilization pathway of Escherichia coli: identification of a novel phosphate binding motif within a TIM barrel fold.
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J Bacteriol,
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PDB codes:
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S.Choul-Li,
H.Adams,
F.Pattus,
and
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Visualization of interactions between siderophore transporters and the energizing protein TonB by native PAGE.
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Electrophoresis,
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T.Dong,
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and
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RpoS regulation of gene expression during exponential growth of Escherichia coli K12.
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Mol Genet Genomics,
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W.A.Kaserer,
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M.Bauler,
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S.M.Newton,
and
P.E.Klebba
(2008).
Insight from TonB hybrid proteins into the mechanism of iron transport through the outer membrane.
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| |
J Bacteriol,
190,
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A.D.Ferguson,
C.A.Amezcua,
N.M.Halabi,
Y.Chelliah,
M.K.Rosen,
R.Ranganathan,
and
J.Deisenhofer
(2007).
Signal transduction pathway of TonB-dependent transporters.
|
| |
Proc Natl Acad Sci U S A,
104,
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PDB codes:
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C.R.Raetz,
C.M.Reynolds,
M.S.Trent,
and
R.E.Bishop
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Lipid A modification systems in gram-negative bacteria.
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Annu Rev Biochem,
76,
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C.S.López,
and
J.H.Crosa
(2007).
Characterization of ferric-anguibactin transport in Vibrio anguillarum.
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| |
Biometals,
20,
393-403.
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D.Sil,
A.Shrestha,
M.R.Kimbrell,
T.B.Nguyen,
A.K.Adisechan,
R.Balakrishna,
B.G.Abbo,
S.Malladi,
K.A.Miller,
S.Short,
J.R.Cromer,
S.Arora,
A.Datta,
and
S.A.David
(2007).
Bound to shock: protection from lethal endotoxemic shock by a novel, nontoxic, alkylpolyamine lipopolysaccharide sequestrant.
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| |
Antimicrob Agents Chemother,
51,
2811-2819.
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E.Boix,
and
M.V.Nogués
(2007).
Mammalian antimicrobial proteins and peptides: overview on the RNase A superfamily members involved in innate host defence.
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| |
Mol Biosyst,
3,
317-335.
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E.Cascales,
S.K.Buchanan,
D.Duché,
C.Kleanthous,
R.Lloubès,
K.Postle,
M.Riley,
S.Slatin,
and
D.Cavard
(2007).
Colicin biology.
|
| |
Microbiol Mol Biol Rev,
71,
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H.Li,
S.Grass,
T.Wang,
T.Liu,
and
J.W.St Geme
(2007).
Structure of the Haemophilus influenzae HMW1B translocator protein: evidence for a twin pore.
|
| |
J Bacteriol,
189,
7497-7502.
|
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so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
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