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TitleVik1 modulates microtubule-Kar3 interactions through a motor domain that lacks an active site.
Journal, issue, pagesCell(Cambridge,Mass. ), Vol. 128, Page 1161-1172, Year 2007
Publish dateNov 27, 2006 (structure data deposition date)
AuthorsAllingham, J.S. / Sproul, L.R. / Rayment, I. / Gilbert, S.P.
External linksCell(Cambridge,Mass. ) / PubMed:17382884
MethodsX-ray diffraction
Resolution1.6 Å
Structure data

PDB-2o0a:
The structure of the C-terminal domain of Vik1 has a motor domain fold but lacks a nucleotide-binding site.
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsCELL CYCLE/TRANSPORT PROTEIN / Vik1 / motor homology domain / kinesin / motor domain / microtubule-binding / Kinesin-14 / heterodimer / CELL CYCLE-TRANSPORT PROTEIN COMPLEX

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