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Structure paper

TitleElucidation of the anti-autophagy mechanism of the Legionella effector RavZ using semisynthetic LC3 proteins.
Journal, issue, pagesElife, Vol. 6, Year 2017
Publish dateDec 30, 2016 (structure data deposition date)
AuthorsYang, A. / Pantoom, S. / Wu, Y.W.
External linksElife / PubMed:28395732
MethodsX-ray diffraction
Resolution1.53 - 2.85 Å
Structure data

PDB-5ms2:
Crystal structure of the Legionella pneumophila effector protein RavZ in complex with human LC3B
Method: X-RAY DIFFRACTION / Resolution: 2.47 Å

PDB-5ms5:
Low-salt structure of RavZ LIR2-fused human LC3B
Method: X-RAY DIFFRACTION / Resolution: 1.53 Å

PDB-5ms6:
High-salt structure of RavZ LIR2-fused human LC3B
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-5ms7:
Crystal structure of the legionella pneumophila effector protein RavZ_20-502
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-5ms8:
Crystal structure of the legionella pneumophila effector protein RavZ_1-487
Method: X-RAY DIFFRACTION / Resolution: 2.85 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-BA:
Unknown entry

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

Source
  • legionella pneumophila subsp. pneumophila str. philadelphia 1 (bacteria)
  • homo sapiens (human)
  • legionella pneumophila (bacteria)
  • legionella pneumophila subsp. pneumophila atcc 33215 (bacteria)
KeywordsHYDROLASE / Autophagy / Host-pathogen interaction / PROTEIN BINDING / Autophagy / Host-pathogen interaction / Protein binding /RavZ / LIR / LC3 / Hydrolase / Autophagy / Legionella pneumophila effector protein / ATG8 deconjugating enzyme

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