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PDBsum entry 5xdn
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Membrane protein
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PDB id
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5xdn
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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 human voltage-dependent anion channel 1 (hvdac1) in p22121 space group
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Structure:
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Voltage-dependent anion-selective channel protein 1. Chain: a, b. Synonym: hvdac1,outer mitochondrial membrane protein porin 1, plasmalemmal porin,porin 31hl,porin 31hm. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: vdac1, vdac. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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3.15Å
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R-factor:
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0.267
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R-free:
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0.300
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Authors:
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T.Hosaka,T.Kimura-Someya,M.Shirouzu
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Key ref:
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T.Hosaka
et al.
(2017).
Crystal structural characterization reveals novel oligomeric interactions of human voltage-dependent anion channel 1.
Protein Sci,
26,
1749-1758.
PubMed id:
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Date:
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28-Mar-17
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Release date:
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28-Jun-17
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PROCHECK
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Headers
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References
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P21796
(VDAC1_HUMAN) -
Voltage-dependent anion-selective channel protein 1 from Homo sapiens
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Seq:
Struc:
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283 a.a.
278 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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Protein Sci
26:1749-1758
(2017)
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PubMed id:
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Crystal structural characterization reveals novel oligomeric interactions of human voltage-dependent anion channel 1.
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T.Hosaka,
M.Okazaki,
T.Kimura-Someya,
Y.Ishizuka-Katsura,
K.Ito,
S.Yokoyama,
K.Dodo,
M.Sodeoka,
M.Shirouzu.
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ABSTRACT
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Voltage-dependent anion channel 1 (VDAC1), which is located in the outer
mitochondrial membrane, plays important roles in various cellular processes. For
example, oligomerization of VDAC1 is involved in the release of cytochrome c to
the cytoplasm, leading to apoptosis. However, it is unknown how VDAC1
oligomerization occurs in the membrane. In the present study, we determined
high-resolution crystal structures of oligomeric human VDAC1 (hVDAC1) prepared
by using an Escherichia coli cell-free protein synthesis system, which avoided
the need for denaturation and refolding of the protein. Broad-range screening
using a bicelle crystallization method produced crystals in space groups C222
and P22121, which diffracted to a resolution of 3.10 and
3.15 Å, respectively. Each crystal contained two hVDAC1 protomers in the
asymmetric unit. Dimer within the asymmetrical unit of the crystal in space
group C222 were oriented parallel, whereas those of the crystal in space group
P22121were oriented anti-parallel. From a model of the
crystal in space group C222, which we constructed by using crystal symmetry
operators, a heptameric structure with eight patterns of interaction between
protomers, including hydrophobic interactions with β-strands, hydrophilic
interactions with loop regions, and protein-lipid interactions, was observed. It
is possible that by having multiple patterns of interaction, VDAC1 can form
homo- or hetero-oligomers not only with other VDAC1 protomers but also with
other proteins such as VDAC2, VDAC3 and apoptosis-regulating proteins in the
Bcl-2 family.
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Links
