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Contents |
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(+ 5 more)
237 a.a.
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252 a.a.
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* Residue conservation analysis
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PDB id:
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Membrane protein
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Title:
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Crystal structure of the membrane fusion protein, mexa of the multidrug transporter
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Structure:
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Multidrug resistance protein mexa. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m. Synonym: membrane fusion protein mexa. Engineered: yes
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Source:
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Pseudomonas aeruginosa. Organism_taxid: 287. Expressed in: pseudomonas aeruginosa. Expression_system_taxid: 287.
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Biol. unit:
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30mer (from
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Resolution:
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2.40Å
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R-factor:
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0.259
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R-free:
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0.282
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Authors:
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H.Akama,T.Matsuura,S.Kashiwagi,H.Yoneyama,T.Tsukihara,A.Nakagawa, T.Nakae
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Key ref:
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H.Akama
et al.
(2004).
Crystal structure of the membrane fusion protein, MexA, of the multidrug transporter in Pseudomonas aeruginosa.
J Biol Chem,
279,
25939-25942.
PubMed id:
DOI:
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Date:
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09-Apr-04
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Release date:
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25-May-04
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PROCHECK
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Headers
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References
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DOI no:
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J Biol Chem
279:25939-25942
(2004)
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PubMed id:
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Crystal structure of the membrane fusion protein, MexA, of the multidrug transporter in Pseudomonas aeruginosa.
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H.Akama,
T.Matsuura,
S.Kashiwagi,
H.Yoneyama,
S.Narita,
T.Tsukihara,
A.Nakagawa,
T.Nakae.
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ABSTRACT
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The MexAB-OprM efflux pump of Pseudomonas aeruginosa is central to multidrug
resistance of this organism, which infects immunocompromised hospital patients.
The MexA, MexB, and OprM subunits were assumed to function as the membrane
fusion protein, the body of the transporter, and the outer membrane channel
protein, respectively. For better understanding of this important xenobiotic
transporter, we show the x-ray crystallographic structure of MexA at a
resolution of 2.40 A. The global MexA structure showed unforeseen new features
with a spiral assembly of six and seven protomers that were joined together at
one end by a pseudo 2-fold image. The protomer showed a new protein structure
with a tandem arrangement consisting of at least three domains and presumably
one more. The rod domain had a long hairpin of twisted coiled-coil that extended
to one end. The second domain adjacent to the rod alpha-helical domain was
globular and constructed by a cluster of eight short beta-sheets. The third
domain located distal to the alpha-helical rod was globular and composed of
seven short beta-sheets and one short alpha-helix. The 13-mer was shaped like a
woven rattan cylinder with a large internal tubular space and widely opened
flared ends. The 6-mer and 7-mer had a funnel-like structure consisting of a
tubular rod at one side and a widely opened flared funnel top at the other side.
Based on these results, we constructed a model of the MexAB-OprM pump assembly.
The three pairs of MexA dimers interacted with the periplasmic alpha-barrel
domain of OprM via the alpha-helical hairpin, the second domain interacted with
both MexB and OprM at their contact site, and the third and disordered domains
probably interacted with the distal domain of MexB. In this fashion, the MexA
subunit connected MexB and OprM, indicating that MexA is the membrane bridge
protein.
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Selected figure(s)
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Figure 2.
FIG. 2. Stereo view of the MexA monomer. Ribbon model of
the MexA monomer: gradient rainbow color of blue to red
indicates N- to C-terminal.
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Figure 3.
FIG. 3. Ribbon diagrams of a representative MexA structure.
A, stereo side view of the structure of the tridecamer. Heptamer
and hexamer are colored red and blue, respectively. B, bottom
view of Fig. 1A (hexamer). Each monomer is distinguished by
alternatively changing the color to blue and gray, respectively.
C, top view of Fig. 1A (heptamer). Each monomer is distinguished
by alternatively changing the color to red and gray,
respectively. The figures were drawn by MolScript version 2.1.2
(40) and Raster 3D version 2.7b (41).
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2004,
279,
25939-25942)
copyright 2004.
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Figures were
selected
by the author.
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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.C.Su,
F.Long,
and
E.W.Yu
(2011).
The Cus efflux system removes toxic ions via a methionine shuttle.
|
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Protein Sci,
20,
6.
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|
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C.C.Su,
F.Long,
M.T.Zimmermann,
K.R.Rajashankar,
R.L.Jernigan,
and
E.W.Yu
(2011).
Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli.
|
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Nature,
470,
558-562.
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PDB code:
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A.Welch,
C.U.Awah,
S.Jing,
H.W.van Veen,
and
H.Venter
(2010).
Promiscuous partnering and independent activity of MexB, the multidrug transporter protein from Pseudomonas aeruginosa.
|
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Biochem J,
430,
355-364.
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|
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E.Perrin,
M.Fondi,
M.C.Papaleo,
I.Maida,
S.Buroni,
M.R.Pasca,
G.Riccardi,
and
R.Fani
(2010).
Exploring the HME and HAE1 efflux systems in the genus Burkholderia.
|
| |
BMC Evol Biol,
10,
164.
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F.De Angelis,
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J.M.Ruysschaert,
R.M.Stroud,
and
G.Vandenbussche
(2010).
Metal-induced conformational changes in ZneB suggest an active role of membrane fusion proteins in efflux resistance systems.
|
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Proc Natl Acad Sci U S A,
107,
11038-11043.
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PDB code:
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F.Long,
C.C.Su,
M.T.Zimmermann,
S.E.Boyken,
K.R.Rajashankar,
R.L.Jernigan,
and
E.W.Yu
(2010).
Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport.
|
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Nature,
467,
484-488.
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PDB codes:
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H.M.Kim,
Y.Xu,
M.Lee,
S.Piao,
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and
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(2010).
Functional relationships between the AcrA hairpin tip region and the TolC aperture tip region for the formation of the bacterial tripartite efflux pump AcrAB-TolC.
|
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J Bacteriol,
192,
4498-4503.
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|
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|
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H.Yoneyama,
K.Akiba,
H.Hori,
T.Ando,
and
T.Nakae
(2010).
Tat pathway-mediated translocation of the sec pathway substrate protein MexA, an inner membrane component of the MexAB-OprM xenobiotic extrusion pump in Pseudomonas aeruginosa.
|
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Antimicrob Agents Chemother,
54,
1492-1497.
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A.Mikolay,
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The ABC-transporter AtmA is involved in nickel and cobalt resistance of Cupriavidus metallidurans strain CH34.
|
| |
Antonie Van Leeuwenhoek,
96,
183-191.
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and
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(2009).
Crystal structure of the membrane fusion protein CusB from Escherichia coli.
|
| |
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393,
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PDB codes:
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E.B.Tikhonova,
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and
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|
| |
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J Bacteriol,
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|
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PDB code:
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|
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|
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|
| |
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| |
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| |
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| |
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| |
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| |
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| |
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|
| |
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443,
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PDB codes:
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A.L.Pimenta,
K.Racher,
L.Jamieson,
M.A.Blight,
and
I.B.Holland
(2005).
Mutations in HlyD, part of the type 1 translocator for hemolysin secretion, affect the folding of the secreted toxin.
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| |
J Bacteriol,
187,
7471-7480.
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D.Nehme,
and
K.Poole
(2005).
Interaction of the MexA and MexB components of the MexAB-OprM multidrug efflux system of Pseudomonas aeruginosa: identification of MexA extragenic suppressors of a T578I mutation in MexB.
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| |
Antimicrob Agents Chemother,
49,
4375-4378.
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E.W.Yu,
J.R.Aires,
G.McDermott,
and
H.Nikaido
(2005).
A periplasmic drug-binding site of the AcrB multidrug efflux pump: a crystallographic and site-directed mutagenesis study.
|
| |
J Bacteriol,
187,
6804-6815.
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|
PDB codes:
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G.Grass,
B.Fricke,
and
D.H.Nies
(2005).
Control of expression of a periplasmic nickel efflux pump by periplasmic nickel concentrations.
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| |
Biometals,
18,
437-448.
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H.Akama,
M.Kanemaki,
T.Tsukihara,
A.Nakagawa,
and
T.Nakae
(2005).
Preliminary crystallographic analysis of the antibiotic discharge outer membrane lipoprotein OprM of Pseudomonas aeruginosa with an exceptionally long unit cell and complex lattice structure.
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| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
61,
131-133.
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J.M.Pagès,
M.Masi,
and
J.Barbe
(2005).
Inhibitors of efflux pumps in Gram-negative bacteria.
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Trends Mol Med,
11,
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J.R.Aires,
and
H.Nikaido
(2005).
Aminoglycosides are captured from both periplasm and cytoplasm by the AcrD multidrug efflux transporter of Escherichia coli.
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J Bacteriol,
187,
1923-1929.
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K.G.Wooldridge,
M.Kizil,
D.B.Wells,
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(2005).
Unusual genetic organization of a functional type I protein secretion system in Neisseria meningitidis.
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Infect Immun,
73,
5554-5567.
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O.Lomovskaya,
and
M.Totrov
(2005).
Vacuuming the periplasm.
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J Bacteriol,
187,
1879-1883.
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R.Chuanchuen,
T.Murata,
N.Gotoh,
and
H.P.Schweizer
(2005).
Substrate-dependent utilization of OprM or OpmH by the Pseudomonas aeruginosa MexJK efflux pump.
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Antimicrob Agents Chemother,
49,
2133-2136.
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F.Husain,
M.Humbard,
and
R.Misra
(2004).
Interaction between the TolC and AcrA proteins of a multidrug efflux system of Escherichia coli.
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J Bacteriol,
186,
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H.Gerken,
and
R.Misra
(2004).
Genetic evidence for functional interactions between TolC and AcrA proteins of a major antibiotic efflux pump of Escherichia coli.
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Mol Microbiol,
54,
620-631.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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only a partial list as not all journals are covered by
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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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