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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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PDB id:
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| Name: |
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Membrane protein
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Title:
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Crystal structure of the light-driven sodium pump kr2 in neutral state
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Structure:
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Sodium pumping rhodopsin. Chain: a. Engineered: yes
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Source:
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Dokdonia eikasta. Organism_taxid: 308116. Gene: nar. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.30Å
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R-factor:
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0.197
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R-free:
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0.231
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Authors:
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H.E.Kato,K.Inoue,R.Abe-Yoshizumi,Y.Kato,H.Ono,M.Konno,T.Ishizuka, M.R.Hoque,S.Hososhima,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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Key ref:
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H.E.Kato
et al.
(2015).
Structural basis for Na(+) transport mechanism by a light-driven Na(+) pump.
Nature,
521,
48-53.
PubMed id:
DOI:
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Date:
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18-Jan-15
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Release date:
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08-Apr-15
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PROCHECK
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Headers
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References
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N0DKS8
(N0DKS8_9FLAO) -
Sodium pumping rhodopsin from Dokdonia eikasta
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Seq:
Struc:
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280 a.a.
271 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Nature
521:48-53
(2015)
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PubMed id:
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Structural basis for Na(+) transport mechanism by a light-driven Na(+) pump.
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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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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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