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PDBsum entry 4lp8
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Metal transport
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PDB id
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4lp8
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PDB id:
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| Name: |
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Metal transport
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Title:
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A novel open-state crystal structure of the prokaryotic inward rectifier kirbac3.1
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Structure:
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Inward rectifier potassium channel kirbac3.1. Chain: a. Engineered: yes. Mutation: yes
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Source:
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Magnetospirillum magnetotacticum. Organism_taxid: 188. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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2.46Å
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R-factor:
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0.183
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R-free:
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0.249
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Authors:
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L.Zubcevic,V.N.Bavro,J.R.C.Muniz,M.R.Schmidt,S.Wang,R.De Zorzi, C.Venien-Bryan,M.S.P.Sansom,C.G.Nichols,S.J.Tucker
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Key ref:
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L.Zubcevic
et al.
(2014).
Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains.
J Biol Chem,
289,
143-151.
PubMed id:
DOI:
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Date:
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15-Jul-13
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Release date:
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20-Nov-13
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PROCHECK
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Headers
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References
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D9N164
(IRK10_PARME) -
Inward rectifier potassium channel Kirbac3.1 from Paramagnetospirillum magnetotacticum
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Seq:
Struc:
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295 a.a.
283 a.a.*
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Key: |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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DOI no:
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J Biol Chem
289:143-151
(2014)
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PubMed id:
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Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains.
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L.Zubcevic,
V.N.Bavro,
J.R.Muniz,
M.R.Schmidt,
S.Wang,
R.De Zorzi,
C.Venien-Bryan,
M.S.Sansom,
C.G.Nichols,
S.J.Tucker.
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ABSTRACT
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KirBac channels are prokaryotic homologs of mammalian inwardly rectifying
potassium (Kir) channels, and recent structures of KirBac3.1 have provided
important insights into the structural basis of gating in Kir channels. In this
study, we demonstrate that KirBac3.1 channel activity is strongly pH-dependent,
and we used x-ray crystallography to determine the structural changes that arise
from an activatory mutation (S205L) located in the cytoplasmic domain (CTD).
This mutation stabilizes a novel energetically favorable open conformation in
which changes at the intersubunit interface in the CTD also alter the
electrostatic potential of the inner cytoplasmic cavity. These results provide a
structural explanation for the activatory effect of this mutation and provide a
greater insight into the role of the CTD in Kir channel gating.
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Links
