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PDBsum entry 2w2e
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Membrane protein
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PDB id
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2w2e
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Contents |
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* Residue conservation analysis
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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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1.15 angstrom crystal structure of p.Pastoris aquaporin, aqy1, in a closed conformation at ph 3.5
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Structure:
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Aquaporin pip2-7 7. Chain: a. Synonym: aqy1, aquaporin
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Source:
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Komagataella pastoris. Organism_taxid: 4922. Strain: x33
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Resolution:
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1.15Å
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R-factor:
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0.140
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R-free:
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0.165
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Authors:
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G.Fischer,U.Kosinska-Eriksson,C.Aponte-Santamaria,M.Palmgren, C.Geijer,K.Hedfalk,S.Hohmann,B.L.De Groot,R.Neutze,K.Lindkvist- Petersson
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Key ref:
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G.Fischer
et al.
(2009).
Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism.
Plos Biol,
7,
e1000130.
PubMed id:
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Date:
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29-Oct-08
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Release date:
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16-Jun-09
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PROCHECK
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Headers
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References
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F2QVG4
(F2QVG4_KOMPC) -
Aquaporin-1 from Komagataella phaffii (strain ATCC 76273 / CBS 7435 / CECT 11047 / NRRL Y-11430 / Wegner 21-1)
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Seq:
Struc:
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279 a.a.
263 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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Plos Biol
7:e1000130
(2009)
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PubMed id:
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Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism.
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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,
K.Lindkvist-Petersson.
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ABSTRACT
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Aquaporins are transmembrane proteins that facilitate the flow of water through
cellular membranes. An unusual characteristic of yeast aquaporins is that they
frequently contain an extended N terminus of unknown function. Here we present
the X-ray structure of the yeast aquaporin Aqy1 from Pichia pastoris at 1.15 A
resolution. Our crystal structure reveals that the water channel is closed by
the N terminus, which arranges as a tightly wound helical bundle, with Tyr31
forming H-bond interactions to a water molecule within the pore and thereby
occluding the channel entrance. Nevertheless, functional assays show that Aqy1
has appreciable water transport activity that aids survival during rapid
freezing of P. pastoris. These findings establish that Aqy1 is a gated water
channel. Mutational studies in combination with molecular dynamics simulations
imply that gating may be regulated by a combination of phosphorylation and
mechanosensitivity.
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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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A.B.Waight,
J.Love,
and
D.N.Wang
(2010).
Structure and mechanism of a pentameric formate channel.
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Nat Struct Mol Biol,
17,
31-37.
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PDB codes:
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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
codes are
shown on the right.
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Links
