ArticleThe Journal of biological chemistry2013
Conformational plasticity and ligand binding of bacterial monoacylglycerol lipase.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 54 citations in OpenAlex.
- Similar but Distinct-Biochemical Characterization of the Staphylococcus aureus Serine Hydrolases FphH and FphI.Proteins · 2025Article
- Discovery of a non-canonical prototype long-chain monoacylglycerol lipase through a structure-based endogenous reaction intermediate complex.Nature communications · 2023Article
- Structural and Biochemical Insights into Bis(2-hydroxyethyl) Terephthalate Degrading Carboxylesterase Isolated from Psychrotrophic BacteriumInternational journal of molecular sciences · 2023Article
- Recent Advances in the Enzymatic Synthesis of Polyester.Polymers · 2022Review
- Surviving in the Brine: A Multi-Omics Approach for Understanding the Physiology of the Halophile FungusFrontiers in microbiology · 2022Article
- Structural Changes in the Cap of Rv0183/mtbMGL Modulate the Shape of the Binding Pocket.Biomolecules · 2021Article
- Biodegradation of used polyethylene bags by a new marine strain of Alcaligenes faecalis LNDR-1.Environmental science and pollution research international · 2021Article
- Structure and Dynamics of an Archeal Monoglyceride Lipase fromBiomolecules · 2021Article
- Study on a Novel Cold-Active and Halotolerant Monoacylglycerol Lipase Widespread in Marine Bacteria Reveals a New Group of Bacterial Monoacylglycerol Lipases Containing Unusual C(A/S)HSMG Catalytic Motifs.Frontiers in microbiology · 2020Article
- The crystal structure of monoacylglycerol lipase from M. tuberculosis reveals the basis for specific inhibition.Scientific reports · 2018Article
- Effects of Distal Mutations on the Structure, Dynamics and Catalysis of Human Monoacylglycerol Lipase.Scientific reports · 2018Article
- The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties.Frontiers in bioengineering and biotechnology · 2017Review
- Bacillus sp. JR3 esterase LipJ: A new mesophilic enzyme showing traces of a thermophilic past.PloS one · 2017Article
- Classification of ligand molecules in PDB with graph match-based structural superposition.Journal of structural and functional genomics · 2016Article
- Gene Cloning and Characterization of the Geobacillus thermoleovorans CCR11 Carboxylesterase CaesCCR11, a New Member of Family XV.Molecular biotechnology · 2016Article
- Purification, crystallization and preliminary X-ray diffraction analysis of a soluble variant of the monoglyceride lipase Yju3p from the yeast Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Selection and screening of microbial consortia for efficient and ecofriendly degradation of plastic garbage collected from urban and rural areas of Bangalore, India.Environmental monitoring and assessment · 2015Article
- Anatomy of enzyme channels.BMC bioinformatics · 2014Article
- 2012 Division of medicinal chemistry award address. Trekking the cannabinoid road: a personal perspective.Journal of medicinal chemistry · 2014Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Monoacylglycerol lipases (MGLs) play an important role in lipid catabolism across all kingdoms of life by catalyzing the release of free fatty acids from monoacylglycerols. The three-dimensional structures of human and a bacterial MGL were determined only recently as the first members of this lipase family. In addition to the α/β-hydrolase core, they showed unexpected structural similarities even in the cap region. Nevertheless, the structural basis for substrate binding and conformational changes of MGLs is poorly understood. Here, we present a comprehensive study of five crystal structures of MGL from Bacillus sp. H257 in its free form and in complex with different substrate analogs and the natural substrate 1-lauroylglycerol. The occurrence of different conformations reveals a high degree of conformational plasticity of the cap region. We identify a specific residue, Ile-145, that might act as a gatekeeper restricting access to the binding site. Site-directed mutagenesis of Ile-145 leads to significantly reduced hydrolase activity. Bacterial MGLs in complex with 1-lauroylglycerol, myristoyl, palmitoyl, and stearoyl substrate analogs enable identification of the binding sites for the alkyl chain and the glycerol moiety of the natural ligand. They also provide snapshots of the hydrolytic reaction of a bacterial MGL at different stages. The alkyl chains are buried in a hydrophobic tunnel in an extended conformation. Binding of the glycerol moiety is mediated via Glu-156 and water molecules. Analysis of the structural features responsible for cap plasticity and the binding modes of the ligands suggests conservation of these features also in human MGL.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.