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Structure paper

TitleThe dynamic nature of the VDAC1 channels in bilayers as revealed by two crystal structures of the human isoform in bicelles at 2.7 and 3.3 Angstrom resolution: implications for VDAC1 voltage-dependent mechanism and for its oligomerization
Journal, issue, pagesTo Be Published
Publish dateApr 3, 2018 (structure data deposition date)
AuthorsRazeto, A. / Gribbon, P. / Loew, C.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution2.74 - 3.27 Å
Structure data

PDB-6g6u:
The dynamic nature of the VDAC1 channels in bilayers: human VDAC1 at 2.7 Angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 2.74 Å

PDB-6g73:
The dynamic nature of the VDAC1 channels in bilayers: human VDAC1 at 3.3 Angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 3.27 Å

Chemicals

ChemComp-MC3:
1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

ChemComp-NO3:
NITRATE ION

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / ion-channel / B-barrel / outer mitochondrial membrane / cytochrome c release / APOPTOSIS

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