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Structure paper

TitleStructure-function relationships underpin disulfide loop cleavage-dependent activation of Legionella pneumophila lysophospholipase A PlaA.
Journal, issue, pagesMol. Microbiol., Vol. 121, Page 497-512, Year 2024
Publish dateJun 2, 2022 (structure data deposition date)
AuthorsHiller, M. / Diwo, M. / Wamp, S. / Gutsmann, T. / Lang, C. / Blankenfeldt, W. / Flieger, A.
External linksMol. Microbiol. / PubMed:38130174
MethodsX-ray diffraction
Resolution1.45 - 2.36 Å
Structure data

PDB-8a24:
Lysophospholipase PlaA from Legionella pneumophila str. Corby - iodide soak
Method: X-RAY DIFFRACTION / Resolution: 2.36 Å

PDB-8a25:
Lysophospholipase PlaA from Legionella pneumophila str. Corby - complex with PEG fragment
Method: X-RAY DIFFRACTION / Resolution: 1.73 Å

PDB-8a26:
Lysophospholipase PlaA from Legionella pneumophila str. Corby - complex with palmitate
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

Chemicals

ChemComp-IOD:
IODIDE ION

ChemComp-HOH:
WATER

ChemComp-MLA:
MALONIC ACID

ChemComp-BU3:
(R,R)-2,3-BUTANEDIOL

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-PLM:
PALMITIC ACID

Source
  • legionella pneumophila str. corby (bacteria)
KeywordsHYDROLASE / phospholipase / virulence / single anomalous diffraction

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