(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Archaea: NE > Euryarchaeota: NE > Thermococci: NE > Thermococcales: NE > Thermococcaceae: NE > Palaeococcus: NE > Palaeococcus ferrophilus: NE
Molecular evidence
Database
No mutation 1 structure: 6QE2: Crystal structure of Palaeococcus ferrophilus monoacylglycerol lipase No kinetic
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MELYRAKFGTPERGWVVLVHGLGEHSGRYGKLIELLNGAGFGVYAFDWPG HGKSPGKRGHTSVEEAMKIIDSIIEELGEKPFLFGHSLGGLTVIRYAETR PDKIMGVVASSPALAKSPKTPSFMVALAKVLGRITPGLSLSNGLDPKLLS RNPDAVKRYIEDPLVHDRISGKLGMSVFDNMERAHKEAERIKAPVLLLVG TADIITPPEGSRRLFEELKVKDKTIMEFKGAYHEIFEDPEWGEEFHRAIV EWLVSHSRGDLEWASAERASSIMGD
Reference
Title: Structure and Dynamics of an Archeal Monoglyceride Lipase from Palaeococcus ferrophilus as Revealed by Crystallography and In Silico Analysis Labar G, Brandt N, Flaba A, Wouters J, Leherte L Ref: Biomolecules, 11:533, 2021 : PubMed
The crystallographic analysis of a lipase from Palaeococcus ferrophilus (PFL) previously annotated as a lysophospholipase revealed high structural conservation with other monoglyceride lipases, in particular in the lid domain and substrate binding pockets. In agreement with this observation, PFL was shown to be active on various monoacylglycerols. Molecular Dynamics (MD) studies performed in the absence and in the presence of ligands further allowed characterization of the dynamics of this system and led to a systematic closure of the lid compared to the crystal structure. However, the presence of ligands in the acyl-binding pocket stabilizes intermediate conformations compared to the crystal and totally closed structures. Several lid-stabilizing or closure elements were highlighted, i.e., hydrogen bonds between Ser117 and Ile204 or Asn142 and its facing amino acid lid residues, as well as Phe123. Thus, based on this complementary crystallographic and MD approach, we suggest that the crystal structure reported herein represents an open conformation, at least partially, of the PFL, which is likely stabilized by the ligand, and it brings to light several key structural features prone to participate in the closure of the lid.
Palaeococcus ferrophilus monoacylglycerol lipase
