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PDBsum entry 1sor
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Membrane protein
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PDB id
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1sor
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Contents |
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* Residue conservation analysis
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DOI no:
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Nature
429:193-197
(2004)
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PubMed id:
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Aquaporin-0 membrane junctions reveal the structure of a closed water pore.
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T.Gonen,
P.Sliz,
J.Kistler,
Y.Cheng,
T.Walz.
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ABSTRACT
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The lens-specific water pore aquaporin-0 (AQP0) is the only aquaporin known to
form membrane junctions in vivo. We show here that AQP0 from the lens core,
containing some carboxy-terminally cleaved AQP0, forms double-layered crystals
that recapitulate in vivo junctions. We present the structure of the AQP0
membrane junction as determined by electron crystallography. The junction is
formed by three localized interactions between AQP0 molecules in adjoining
membranes, mainly mediated by proline residues conserved in AQP0s from different
species but not present in most other aquaporins. Whereas all previously
determined aquaporin structures show the pore in an open conformation, the water
pore is closed in AQP0 junctions. The water pathway in AQP0 also contains an
additional pore constriction, not seen in other known aquaporin structures,
which may be responsible for pore gating.
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Selected figure(s)
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Figure 2.
Figure 2: The AQP0-mediated membrane junction. a, Ribbon
representation of the membrane junction with the positions of
the two membranes indicated in yellow. b, The Pro 38 residues
contributed by all eight AQP0 subunits in the two interacting
tetramers. c, Corresponding area of the 2F[o] -F[c]map. d, The C
loops connect each AQP0 molecule to two molecules in the
opposite membrane. Letters A to D refer to the molecules
described in the text. e, Corresponding area of the 2F[o] -F[c]
map. Panels a, b and d were created with Chimera^29 and panels c
and e with the program O28.
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Figure 3.
Figure 3: The closed AQP0 water pore. a, b, Side chains
lining the pores in AQP1 (a) and AQP0 (b). c, The left panel
shows pore profiles for AQP0 (red) and AQP1 (green) generated
with the program 'HOLE'. The positions of the NPA motifs, the
ar/R constriction site in AQP1 and the two constriction sites in
AQP0 (CS-I, CS-II) are marked and shown in red. The pore
profiles are aligned with the models of AQP1 (middle panel) and
AQP0 (right panel). Panels a and b were created with Chimera^29.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2004,
429,
193-197)
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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D.Strugatsky,
R.McNulty,
K.Munson,
C.K.Chen,
S.M.Soltis,
G.Sachs,
and
H.Luecke
(2013).
Structure of the proton-gated urea channel from the gastric pathogen Helicobacter pylori.
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Nature,
493,
255-258.
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PDB code:
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L.A.Khan,
H.Zhang,
N.Abraham,
L.Sun,
J.T.Fleming,
M.Buechner,
D.H.Hall,
and
V.Gobel
(2012).
Intracellular lumen extension requires ERM-1-dependent apical membrane expansion and AQP-8-mediated flux.
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Nat Cell Biol,
15,
143-156.
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H.Wang,
and
K.H.Downing
(2011).
Specimen preparation for electron diffraction of thin crystals.
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Micron,
42,
132-140.
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L.Xin,
H.Su,
C.H.Nielsen,
C.Tang,
J.Torres,
and
Y.Mu
(2011).
Water permeation dynamics of AqpZ: A tale of two states.
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Biochim Biophys Acta,
1808,
1581-1586.
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M.Kusayama,
K.Wada,
M.Nagata,
S.Ishimoto,
H.Takahashi,
M.Yoneda,
A.Nakajima,
M.Okura,
M.Kogo,
and
Y.Kamisaki
(2011).
Critical role of aquaporin 3 on growth of human esophageal and oral squamous cell carcinoma.
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Cancer Sci,
102,
1128-1136.
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S.Bassnett,
Y.Shi,
and
G.F.Vrensen
(2011).
Biological glass: structural determinants of eye lens transparency.
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Philos Trans R Soc Lond B Biol Sci,
366,
1250-1264.
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C.Jin,
J.Jiang,
W.Wang,
and
K.Yao
(2010).
Identification of a MIP mutation that activates a cryptic acceptor splice site in the 3' untranslated region.
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Mol Vis,
16,
2253-2258.
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H.Zheng,
J.Taraska,
A.J.Merz,
and
T.Gonen
(2010).
The prototypical H+/galactose symporter GalP assembles into functional trimers.
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J Mol Biol,
396,
593-601.
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K.R.Vinothkumar,
and
R.Henderson
(2010).
Structures of membrane proteins.
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Q Rev Biophys,
43,
65.
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R.K.Hite,
Z.Li,
and
T.Walz
(2010).
Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals.
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EMBO J,
29,
1652-1658.
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PDB code:
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W.Wang,
J.Jiang,
Y.Zhu,
J.Li,
C.Jin,
X.Shentu,
and
K.Yao
(2010).
A novel mutation in the major intrinsic protein (MIP) associated with autosomal dominant congenital cataracts in a Chinese family.
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Mol Vis,
16,
534-539.
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Y.Wang,
and
E.Tajkhorshid
(2010).
Nitric oxide conduction by the brain aquaporin AQP4.
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Proteins,
78,
661-670.
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Z.Li,
R.K.Hite,
Y.Cheng,
and
T.Walz
(2010).
Evaluation of imaging plates as recording medium for images of negatively stained single particles and electron diffraction patterns of two-dimensional crystals.
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J Electron Microsc (Tokyo),
59,
53-63.
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Z.Zhang,
Z.Chen,
Y.Song,
P.Zhang,
J.Hu,
and
C.Bai
(2010).
Expression of aquaporin 5 increases proliferation and metastasis potential of lung cancer.
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J Pathol,
221,
210-220.
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A.B.Gupta,
and
R.Sankararamakrishnan
(2009).
Genome-wide analysis of major intrinsic proteins in the tree plant Populus trichocarpa: characterization of XIP subfamily of aquaporins from evolutionary perspective.
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BMC Plant Biol,
9,
134.
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D.G.Morgan,
Q.M.Ramasse,
and
N.D.Browning
(2009).
Application of two-dimensional crystallography and image processing to atomic resolution Z-contrast images.
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J Electron Microsc (Tokyo),
58,
223-244.
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G.Benga
(2009).
Water channel proteins (later called aquaporins) and relatives: past, present, and future.
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IUBMB Life,
61,
112-133.
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G.Fischer,
U.Kosinska-Eriksson,
C.Aponte-Santamaría,
M.Palmgren,
C.Geijer,
K.Hedfalk,
S.Hohmann,
B.L.de Groot,
R.Neutze,
and
K.Lindkvist-Petersson
(2009).
Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism.
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PLoS Biol,
7,
e1000130.
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PDB codes:
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H.Wang,
J.Gao,
X.Sun,
F.J.Martinez-Wittinghan,
L.Li,
K.Varadaraj,
M.Farrell,
V.N.Reddy,
T.W.White,
and
R.T.Mathias
(2009).
The Effects of GPX-1 Knockout on Membrane Transport and Intracellular Homeostasis in the Lens.
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J Membr Biol,
227,
25-37.
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S.Bassnett,
P.A.Wilmarth,
and
L.L.David
(2009).
The membrane proteome of the mouse lens fiber cell.
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Mol Vis,
15,
2448-2463.
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S.Mangenot,
N.Buzhynskyy,
J.F.Girmens,
and
S.Scheuring
(2009).
Malformation of junctional microdomains in cataract lens membranes from a type II diabetes patient.
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Pflugers Arch,
457,
1265-1274.
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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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Annu Rev Biophys,
38,
89.
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Ã.˜.Jacobsen,
J.Klaveness,
O.Petter Ottersen,
M.R.Amiry-Moghaddam,
and
P.Rongved
(2009).
Synthesis of cyclic peptide analogues of the 3(10) helical Pro138-Gly144 segment of human aquaporin-4 by olefin metathesis.
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Org Biomol Chem,
7,
1599-1611.
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A.Engel,
Y.Fujiyoshi,
T.Gonen,
and
T.Walz
(2008).
Junction-forming aquaporins.
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Curr Opin Struct Biol,
18,
229-235.
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A.S.Verkman,
J.Ruiz-Ederra,
and
M.H.Levin
(2008).
Functions of aquaporins in the eye.
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Prog Retin Eye Res,
27,
420-433.
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E.J.Kamsteeg,
P.J.Savelkoul,
G.Hendriks,
I.B.Konings,
N.M.Nivillac,
A.K.Lagendijk,
P.van der Sluijs,
and
P.M.Deen
(2008).
Missorting of the Aquaporin-2 mutant E258K to multivesicular bodies/lysosomes in dominant NDI is associated with its monoubiquitination and increased phosphorylation by PKC but is due to the loss of E258.
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Pflugers Arch,
455,
1041-1054.
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H.Stahlberg,
and
T.Walz
(2008).
Molecular electron microscopy: state of the art and current challenges.
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ACS Chem Biol,
3,
268-281.
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M.Ã.˜.Jensen,
R.O.Dror,
H.Xu,
D.W.Borhani,
I.T.Arkin,
M.P.Eastwood,
and
D.E.Shaw
(2008).
Dynamic control of slow water transport by aquaporin 0: implications for hydration and junction stability in the eye lens.
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Proc Natl Acad Sci U S A,
105,
14430-14435.
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N.Golestaneh,
J.Fan,
P.Zelenka,
and
A.B.Chepelinsky
(2008).
PKC putative phosphorylation site Ser235 is required for MIP/AQP0 translocation to the plasma membrane.
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Mol Vis,
14,
1006-1014.
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R.Farjo,
W.M.Peterson,
and
M.I.Naash
(2008).
Expression profiling after retinal detachment and reattachment: a possible role for aquaporin-0.
|
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Invest Ophthalmol Vis Sci,
49,
511-521.
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R.Horsefield,
K.Nordén,
M.Fellert,
A.Backmark,
S.Törnroth-Horsefield,
A.C.Terwisscha van Scheltinga,
J.Kvassman,
P.Kjellbom,
U.Johanson,
and
R.Neutze
(2008).
High-resolution x-ray structure of human aquaporin 5.
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Proc Natl Acad Sci U S A,
105,
13327-13332.
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PDB code:
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S.Andrews,
S.L.Reichow,
and
T.Gonen
(2008).
Electron crystallography of aquaporins.
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IUBMB Life,
60,
430-436.
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S.L.Reichow,
and
T.Gonen
(2008).
Noncanonical binding of calmodulin to aquaporin-0: implications for channel regulation.
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Structure,
16,
1389-1398.
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X.Zhang,
E.Settembre,
C.Xu,
P.R.Dormitzer,
R.Bellamy,
S.C.Harrison,
and
N.Grigorieff
(2008).
Near-atomic resolution using electron cryomicroscopy and single-particle reconstruction.
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Proc Natl Acad Sci U S A,
105,
1867-1872.
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Z.H.Zhou
(2008).
Towards atomic resolution structural determination by single-particle cryo-electron microscopy.
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Curr Opin Struct Biol,
18,
218-228.
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A.Bansal,
and
R.Sankararamakrishnan
(2007).
Homology modeling of major intrinsic proteins in rice, maize and Arabidopsis: comparative analysis of transmembrane helix association and aromatic/arginine selectivity filters.
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BMC Struct Biol,
7,
27.
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E.Zelazny,
J.W.Borst,
M.Muylaert,
H.Batoko,
M.A.Hemminga,
and
F.Chaumont
(2007).
FRET imaging in living maize cells reveals that plasma membrane aquaporins interact to regulate their subcellular localization.
|
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Proc Natl Acad Sci U S A,
104,
12359-12364.
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H.Viadiu,
T.Gonen,
and
T.Walz
(2007).
Projection map of aquaporin-9 at 7 A resolution.
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J Mol Biol,
367,
80-88.
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J.Badaut,
J.F.Brunet,
and
L.Regli
(2007).
Aquaporins in the brain: from aqueduct to "multi-duct".
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Metab Brain Dis,
22,
251-263.
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K.L.Németh-Cahalan,
K.Kalman,
A.Froger,
and
J.E.Hall
(2007).
Zinc modulation of water permeability reveals that aquaporin 0 functions as a cooperative tetramer.
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J Gen Physiol,
130,
457-464.
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K.Varadaraj,
S.S.Kumari,
and
R.T.Mathias
(2007).
Functional expression of aquaporins in embryonic, postnatal, and adult mouse lenses.
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Dev Dyn,
236,
1319-1328.
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M.Hashido,
A.Kidera,
and
M.Ikeguchi
(2007).
Water transport in aquaporins: osmotic permeability matrix analysis of molecular dynamics simulations.
|
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Biophys J,
93,
373-385.
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R.K.Hite,
S.Raunser,
and
T.Walz
(2007).
Revival of electron crystallography.
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Curr Opin Struct Biol,
17,
389-395.
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R.T.Mathias,
J.Kistler,
and
P.Donaldson
(2007).
The lens circulation.
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J Membr Biol,
216,
1.
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T.M.Buck,
J.Wagner,
S.Grund,
and
W.R.Skach
(2007).
A novel tripartite motif involved in aquaporin topogenesis, monomer folding and tetramerization.
|
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Nat Struct Mol Biol,
14,
762-769.
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X.Zeng,
B.Gipson,
Z.Y.Zheng,
L.Renault,
and
H.Stahlberg
(2007).
Automatic lattice determination for two-dimensional crystal images.
|
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J Struct Biol,
160,
353-361.
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D.A.Gorelick,
J.Praetorius,
T.Tsunenari,
S.Nielsen,
and
P.Agre
(2006).
Aquaporin-11: a channel protein lacking apparent transport function expressed in brain.
|
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BMC Biochem,
7,
14.
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F.J.Martinez-Wittinghan,
M.Srinivas,
C.Sellitto,
T.W.White,
and
R.T.Mathias
(2006).
Mefloquine effects on the lens suggest cooperative gating of gap junction channels.
|
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J Membr Biol,
211,
163-171.
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F.Magni,
C.Sarto,
D.Ticozzi,
M.Soldi,
N.Bosso,
P.Mocarelli,
and
M.G.Kienle
(2006).
Proteomic knowledge of human aquaporins.
|
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Proteomics,
6,
5637-5649.
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G.Wistow
(2006).
The NEIBank project for ocular genomics: data-mining gene expression in human and rodent eye tissues.
|
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Prog Retin Eye Res,
25,
43-77.
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J.Jiang,
B.V.Daniels,
and
D.Fu
(2006).
Crystal structure of AqpZ tetramer reveals two distinct Arg-189 conformations associated with water permeation through the narrowest constriction of the water-conducting channel.
|
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J Biol Chem,
281,
454-460.
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PDB code:
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J.S.Hub,
and
B.L.de Groot
(2006).
Does CO2 permeate through aquaporin-1?
|
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Biophys J,
91,
842-848.
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J.Yu,
A.J.Yool,
K.Schulten,
and
E.Tajkhorshid
(2006).
Mechanism of gating and ion conductivity of a possible tetrameric pore in aquaporin-1.
|
| |
Structure,
14,
1411-1423.
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K.Hedfalk,
S.Törnroth-Horsefield,
M.Nyblom,
U.Johanson,
P.Kjellbom,
and
R.Neutze
(2006).
Aquaporin gating.
|
| |
Curr Opin Struct Biol,
16,
447-456.
|
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L.Renault,
H.T.Chou,
P.L.Chiu,
R.M.Hill,
X.Zeng,
B.Gipson,
Z.Y.Zhang,
A.Cheng,
V.Unger,
and
H.Stahlberg
(2006).
Milestones in electron crystallography.
|
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J Comput Aided Mol Des,
20,
519-527.
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M.Ã.˜.Jensen,
and
O.G.Mouritsen
(2006).
Single-channel water permeabilities of Escherichia coli aquaporins AqpZ and GlpF.
|
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Biophys J,
90,
2270-2284.
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S.Törnroth-Horsefield,
Y.Wang,
K.Hedfalk,
U.Johanson,
M.Karlsson,
E.Tajkhorshid,
R.Neutze,
and
P.Kjellbom
(2006).
Structural mechanism of plant aquaporin gating.
|
| |
Nature,
439,
688-694.
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PDB codes:
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A.G.Lee
(2005).
Cell biology: a greasy grip.
|
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Nature,
438,
569-570.
|
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J.B.Artero,
M.Härtlein,
S.McSweeney,
and
P.Timmins
(2005).
A comparison of refined X-ray structures of hydrogenated and perdeuterated rat gammaE-crystallin in H2O and D2O.
|
| |
Acta Crystallogr D Biol Crystallogr,
61,
1541-1549.
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PDB codes:
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J.K.Lee,
D.Kozono,
J.Remis,
Y.Kitagawa,
P.Agre,
and
R.M.Stroud
(2005).
Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 A.
|
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Proc Natl Acad Sci U S A,
102,
18932-18937.
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PDB codes:
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M.Ã.˜.Jensen,
U.Röthlisberger,
and
C.Rovira
(2005).
Hydroxide and proton migration in aquaporins.
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| |
Biophys J,
89,
1744-1759.
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T.Gonen,
Y.Cheng,
P.Sliz,
Y.Hiroaki,
Y.Fujiyoshi,
S.C.Harrison,
and
T.Walz
(2005).
Lipid-protein interactions in double-layered two-dimensional AQP0 crystals.
|
| |
Nature,
438,
633-638.
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|
PDB codes:
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Y.Wang,
K.Schulten,
and
E.Tajkhorshid
(2005).
What makes an aquaporin a glycerol channel? A comparative study of AqpZ and GlpF.
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| |
Structure,
13,
1107-1118.
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J.E.Rash,
K.G.Davidson,
T.Yasumura,
and
C.S.Furman
(2004).
Freeze-fracture and immunogold analysis of aquaporin-4 (AQP4) square arrays, with models of AQP4 lattice assembly.
|
| |
Neuroscience,
129,
915-934.
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L.S.King,
D.Kozono,
and
P.Agre
(2004).
From structure to disease: the evolving tale of aquaporin biology.
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| |
Nat Rev Mol Cell Biol,
5,
687-698.
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W.E.Harries,
D.Akhavan,
L.J.Miercke,
S.Khademi,
and
R.M.Stroud
(2004).
The channel architecture of aquaporin 0 at a 2.2-A resolution.
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| |
Proc Natl Acad Sci U S A,
101,
14045-14050.
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PDB codes:
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Y.Morishita,
Y.Sakube,
S.Sasaki,
and
K.Ishibashi
(2004).
Molecular mechanisms and drug development in aquaporin water channel diseases: aquaporin superfamily (superaquaporins): expansion of aquaporins restricted to multicellular organisms.
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| |
J Pharmacol Sci,
96,
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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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Links
