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Structure paper

TitleStructural analyses of Legionella LepB reveal a new GAP fold that catalytically mimics eukaryotic RasGAP
Journal, issue, pagesCell Res., Vol. 23, Page 775-787, Year 2013
Publish dateMar 26, 2013 (structure data deposition date)
AuthorsYu, Q. / Hu, L. / Yao, Q. / Zhu, Y. / Dong, N. / Wang, D.-C. / Shao, F.
External linksCell Res. / PubMed:23588383
MethodsX-ray diffraction
Resolution2.783 - 3.16 Å
Structure data

PDB-4jvs:
Crystal structure of LepB GAP domain from Legionella drancourtii in complex with Rab1-GDP and AlF3
Method: X-RAY DIFFRACTION / Resolution: 2.783 Å

PDB-4jw1:
Crystal structure of N-terminal 618-residue fragment of LepB from Legionella pneumophila
Method: X-RAY DIFFRACTION / Resolution: 3.16 Å

Chemicals

ChemComp-ACY:
ACETIC ACID

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-AF3:
ALUMINUM FLUORIDE

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GOL:
GLYCEROL

ChemComp-FLC:
CITRATE ANION

Source
  • legionella drancourtii (bacteria)
  • homo sapiens (human)
  • legionella pneumophila (bacteria)
KeywordsHYDROLASE ACTIVATOR/PROTEIN TRANSPORT / New GAP fold / Bind and hydrolyze guanosine triphosphate / Rab1 Binding / HYDROLASE ACTIVATOR-PROTEIN TRANSPORT complex / HYDROLASE ACTIVATOR / GTPase-Accelerating Protein / Rab1

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