6QE2
Crystal structure of Paleococcus ferrophilus monoacylglycerol lipase.
Summary for 6QE2
| Entry DOI | 10.2210/pdb6qe2/pdb |
| Descriptor | Monoacylglycerol lipase, GLYCEROL, LAURYL DIMETHYLAMINE-N-OXIDE, ... (4 entities in total) |
| Functional Keywords | monoacylglycerol lipase, monoglyceride lipase, magl, mgl, hydrolase |
| Biological source | Palaeococcus ferrophilus |
| Total number of polymer chains | 2 |
| Total formula weight | 63535.04 |
| Authors | Labar, G.,Demarez, M.,Brandt, N.,Wouters, J.,Leherte, F. (deposition date: 2019-01-04, release date: 2020-02-05, Last modification date: 2024-01-24) |
| Primary citation | Labar, G.,Brandt, N.,Flaba, A.,Wouters, J.,Leherte, L. Structure and Dynamics of an Archeal Monoglyceride Lipase from Palaeococcus ferrophilus as Revealed by Crystallography and In Silico Analysis. Biomolecules, 11:-, 2021 Cited by PubMed Abstract: The crystallographic analysis of a lipase from (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. PubMed: 33916727DOI: 10.3390/biom11040533 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7461 Å) |
Structure validation
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