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Structure paper

TitlePAAR-repeat proteins sharpen and diversify the type VI secretion system spike.
Journal, issue, pagesNature, Vol. 500, Page 350-353, Year 2013
Publish dateMar 7, 2013 (structure data deposition date)
AuthorsShneider, M.M. / Buth, S.A. / Ho, B.T. / Basler, M. / Mekalanos, J.J. / Leiman, P.G.
External linksNature / PubMed:23925114
MethodsX-ray diffraction
Resolution1.903 - 3.402 Å
Structure data

PDB-4jiv:
VCA0105 PAAR-repeat protein from Vibrio cholerae in complex with a VgrG-like beta-helix that is based on a fragment of T4 gp5
Method: X-RAY DIFFRACTION / Resolution: 1.903 Å

PDB-4jiw:
c1882 PAAR-repeat protein from Escherichia coli in complex with a VgrG-like beta-helix that is based on a fragment of T4 gp5
Method: X-RAY DIFFRACTION / Resolution: 3.402 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-PLM:
PALMITIC ACID

ChemComp-STE:
STEARIC ACID

ChemComp-ELA:
9-OCTADECENOIC ACID

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

Source
  • enterobacteria phage t4 (virus)
  • vibrio cholerae o1 biovar eltor (bacteria)
  • escherichia coli (E. coli)
KeywordsHYDROLASE/PROTEIN BINDING / PAAR-repeat motif / membrane piercing / type VI secretion system / Vibrio cholerae VgrG2 / cell puncturing device / beta-helix / T4 gp5 / VgrG tip / T6SS spike / HYDROLASE-PROTEIN BINDING complex / CFT073 / VgrG protein

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