4q3k

Crystal structure of MGS-M1, an alpha/beta hydrolase enzyme from a Medee basin deep-sea metagenome library

spinqualitylabelsall models 4q3k, resolution 1.57Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4q3k is a 2 chain structure with sequence from Unidentified. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, F, PGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0B5KGV8_9FIRM Publication Abstract from PubMed The present study provides a deeper view of protein functionality as a function of temperature, salt and pressure in deep-sea habitats. A set of eight different enzymes from five distinct deep-sea (3040-4908 m depth), moderately warm (14.0-16.5 degrees C) biotopes, characterized by a wide range of salinities (39-348 practical salinity units), were investigated for this purpose. An enzyme from a 'superficial' marine hydrothermal habitat (65 degrees C) was isolated and characterized for comparative purposes. We report here the first experimental evidence suggesting that in salt-saturated deep-sea habitats, the adaptation to high pressure is linked to high thermal resistance (P value = 0.0036). Salinity might therefore increase the temperature window for enzyme activity, and possibly microbial growth, in deep-sea habitats. As an example, Lake Medee, the largest hypersaline deep-sea anoxic lake of the Eastern Mediterranean Sea, where the water temperature is never higher than 16 degrees C, was shown to contain halopiezophilic-like enzymes that are most active at 70 degrees C and with denaturing temperatures of 71.4 degrees C. The determination of the crystal structures of five proteins revealed unknown molecular mechanisms involved in protein adaptation to poly-extremes as well as distinct active site architectures and substrate preferences relative to other structurally characterized enzymes. Pressure adaptation is linked to thermal adaptation in salt-saturated marine habitats.,Alcaide M, Stogios PJ, Lafraya A, Tchigvintsev A, Flick R, Bargiela R, Chernikova TN, Reva ON, Hai T, Leggewie CC, Katzke N, La Cono V, Matesanz R, Jebbar M, Jaeger KE, Yakimov MM, Yakunin AF, Golyshin PN, Golyshina OV, Savchenko A, Ferrer M Environ Microbiol. 2014 Oct 20. doi: 10.1111/1462-2920.12660. PMID:25330254 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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