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TitleRabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity.
Journal, issue, pagesMol. Cell, Vol. 36, Page 1060-1072, Year 2009
Publish dateSep 23, 2009 (structure data deposition date)
AuthorsSchoebel, S. / Oesterlin, L.K. / Blankenfeldt, W. / Goody, R.S. / Itzen, A.
External linksMol. Cell / PubMed:20064470
MethodsX-ray diffraction
Resolution1.8 Å
Structure data

PDB-3jz9:
Crystal structure of the GEF domain of DrrA/SidM from Legionella pneumophila
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3jza:
Crystal structure of human Rab1b in complex with the GEF domain of DrrA/SidM from Legionella pneumophila
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

Source
  • legionella pneumophila subsp. pneumophila str. philadelphia 1 (bacteria)
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / RabGDI / RabGEF / GDI / GEF / GDF / GDI displacement factor / GTP-binding / Lipoprotein / Membrane / Nucleotide-binding / Prenylation / Protein transport

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