Gene_Locus Report

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Gene_locus Report for: legpn-i7i328

Name Class
legpn-i7i328Name Legionella pneumophila subsp. pneumophila Legionella drancourtii, Phospholipase LpPlaB
SpeciesLegionella pneumophila
Organismbacteria
Gene_name (10)
BlockX
FamilyPlaB
DatabaseSwissProt (5)
Genbank (18)
Trembl (5)
NCBI_TaxID (15)
Paper (11)
CommentLegionella pneumophila possesses a major cell-associated hemolytic phospholipase A (PlaB) which shares no homology to described phospholipases. PlaB preferentially hydrolyzes long-chain fatty acid substrates containing 12 or more carbon atoms. PlaB shows concentration-dependent phospholipase inactivation by tetramerization which may be a mechanism for self-protection. (See Papers Bender et al. 2009 and Kuhle et al. 2014.). The tetramer is a dimer of identical dimers. Diwo et al. found in the structure eight NAD(H) molecules at the dimer/dimer interface, suggesting that these molecules stabilize the tetramer leading to enzyme inactivation (Diwo et al.).The N-Terminal Phospholipase domain is a typical alpha/beta-Hydrolase extended by the non canonical two-stranded beta-sheets beta-6/beta-7 and beta-9/beta-10.. Other strains: Legionella pneumophila Paris; Leg01/20; Leg01/11; Leg01/53; 121004; Thunder Bay; Philadelphia 1 / ATCC 33152 / DSM 7513; Lens; Legionella drancourtii LLAP12; ATCC 43290; serogroup 1 (strain 2300/99 Alcoy); Corby; LPE509
Proteinlegpn-i7i328
Peptidelegpn-i7i328
Structure6ZTH
6ZTI
Inhibitorthio-NAD
SubstrateHeptadecanoylphosphatidylcholine
Dipalmitoylphosphatidylglycerol
Dipalmitoylphosphatidicacid
Dipalmitoylphosphatidylcholine
Tree_nodeAbhydrolase_636917
PlaB286700
Structure299391
OldTrembl (5)

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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