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PDBsum entry 3x3c
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Membrane protein
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PDB id
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3x3c
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References listed in PDB file
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Key reference
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Title
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Structural basis for na(+) transport mechanism by a light-Driven na(+) pump.
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Authors
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H.E.Kato,
K.Inoue,
R.Abe-Yoshizumi,
Y.Kato,
H.Ono,
M.Konno,
S.Hososhima,
T.Ishizuka,
M.R.Hoque,
H.Kunitomo,
J.Ito,
S.Yoshizawa,
K.Yamashita,
M.Takemoto,
T.Nishizawa,
R.Taniguchi,
K.Kogure,
A.D.Maturana,
Y.Iino,
H.Yawo,
R.Ishitani,
H.Kandori,
O.Nureki.
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Ref.
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Nature, 2015,
521,
48-53.
[DOI no: ]
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PubMed id
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Abstract
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Krokinobacter eikastus rhodopsin 2 (KR2) is the first light-driven Na(+) pump
discovered, and is viewed as a potential next-generation optogenetics tool.
Since the positively charged Schiff base proton, located within the
ion-conducting pathway of all light-driven ion pumps, was thought to prohibit
the transport of a non-proton cation, the discovery of KR2 raised the question
of how it achieves Na(+) transport. Here we present crystal structures of KR2
under neutral and acidic conditions, which represent the resting and M-like
intermediate states, respectively. Structural and spectroscopic analyses
revealed the gating mechanism, whereby the flipping of Asp116 sequesters the
Schiff base proton from the conducting pathway to facilitate Na(+) transport.
Together with the structure-based engineering of the first light-driven K(+)
pumps, electrophysiological assays in mammalian neurons and behavioural assays
in a nematode, our studies reveal the molecular basis for light-driven
non-proton cation pumps and thus provide a framework that may advance the
development of next-generation optogenetics.
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