3rm3

Crystal structure of monoacylglycerol lipase from Bacillus sp. H257

spinqualitylabelsall models 3rm3, resolution 1.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rm3 is a 1 chain structure with sequence from Bacillus sp. h-257. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MRD Related: 3rli Activity: Acylglycerol lipase, with EC number 3.1.1.23 Resources: FirstGlance, OCA, RCSB, PDBsum Function [MGLP_BAC25] Hydrolyzes monoacylglycerols, with the highest activity occurring with 1-monolauroylglycerol. Publication Abstract from PubMed Monoacylglycerol lipases (MGLs) catalyse the hydrolysis of monoacylglycerol into free fatty acid and glycerol. MGLs have been identified throughout all genera of life and have adopted different substrate specificities depending on their physiological role. In humans, MGL plays an integral part in lipid metabolism affecting energy homeostasis, signalling processes and cancer cell progression. In bacteria, MGLs degrade short-chain monoacylglycerols which are otherwise toxic to the organism. We report the crystal structures of MGL from the bacterium Bacillus sp. H257 (bMGL) in its free form at 1.2A and in complex with phenylmethylsulfonyl fluoride at 1.8A resolution. In both structures, bMGL adopts an alpha/beta hydrolase fold with a cap in an open conformation. Access to the active site residues, which were unambiguously identified from the protein structure, is facilitated by two different channels. The larger channel constitutes the highly hydrophobic substrate binding pocket with enough room to accommodate monoacylglycerol. The other channel is rather small and resembles the proposed glycerol exit hole in human MGL. Molecular dynamics simulation of bMGL yielded open and closed states of the entrance channel and the glycerol exit hole. Despite differences in the number of residues, secondary structure elements, and low sequence identity in the cap region, this first structure of a bacterial MGL reveals striking structural conservation of the overall cap architecture in comparison with human MGL. Thus it provides insight into the structural conservation of the cap amongst MGLs throughout evolution and provides a framework for rationalising substrate specificities in each organism. The structure of monoacylglycerol lipase from Bacillus sp. H257 reveals unexpected conservation of the cap architecture between bacterial and human enzymes.,Rengachari S, Bezerra GA, Riegler-Berket L, Gruber CC, Sturm C, Taschler U, Boeszoermenyi A, Dreveny I, Zimmermann R, Gruber K, Oberer M Biochim Biophys Acta. 2012 Jul;1821(7):1012-21. Epub 2012 Apr 27. PMID:22561231 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lipase

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