Skip to main content

IMIS

A new integrated search interface will become available in the next phase of marineinfo.org.
For the time being, please use IMIS to search available data

 

[ report an error in this record ]basket (1): add | show Print this page

one publication added to basket [354983]
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. (2021). Structure and dynamics of an archeal monoglyceride lipase from Palaeococcus ferrophilus as revealed by crystallography and in silico analysis. Biomolecules 11(4): 533. https://dx.doi.org/10.3390/biom11040533
In: Biomolecules. MDPI AG: Basel. e-ISSN 2218-273X, more
Peer reviewed article  

Available in  Authors 

Keywords
    Palaeococcus ferrophilus Takai, Sugai, Itoh & Horikoshi, 2000 [WoRMS]
    Marine/Coastal
Author keywords
    monoglyceride lipase; monoacylglycerol lipase; crystallography; molecular dynamics simulation; elastic network model

Authors  Top 
  • Labar, G., more
  • Brandt, N., more
  • Flaba, A.
  • Wouters, J., more
  • Leherte, L.

Abstract
    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.

All data in the Integrated Marine Information System (IMIS) is subject to the VLIZ privacy policy Top | Authors