7b4q

Structure of a cold active HSL family esterase reveals mechanisms of low temperature adaptation and substrate specificity

spinqualitylabelsall models 7b4q, resolution 1.61Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7b4q is a 2 chain structure with sequence from Sutcliffiella cohnii NBRC 15565. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.61Å Ligands: EDO, GOL, MG, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A2K9UV39_9BACI Publication Abstract from PubMed Here we determined the structure of a cold active family IV esterase (EstN7) cloned from Bacillus cohnii strain N1. EstN7 is a dimer with a classical alpha/beta hydrolase fold. It has an acidic surface that is thought to play a role in cold-adaption by retaining solvation under changed water solvent entropy at lower temperatures. The conformation of the functionally important cap region is significantly different to EstN7's closest relatives, forming a bridge-like structure with reduced helical content providing greater access to the active site through more than one substrate access tunnel. However, dynamics do not appear to play a major role in cold adaption. Molecular dynamics at different temperatures, rigidity analysis, normal mode analysis and geometric simulations of motion confirm the flexibility of the cap region but suggest that the rest of the protein is largely rigid. Rigidity analysis indicates the distribution of hydrophobic tethers is appropriate to colder conditions, where the hydrophobic effect is weaker than in mesophilic conditions due to reduced water entropy. Thus, it is likely that increased substrate accessibility and tolerance to changes in water entropy are important for of EstN7's cold adaptation rather than changes in dynamics. Structure and in silico simulations of a cold-active esterase reveals its prime cold-adaptation mechanism.,Noby N, Auhim HS, Winter S, Worthy HL, Embaby AM, Saeed H, Hussein A, Pudney CR, Rizkallah PJ, Wells SA, Jones DD Open Biol. 2021 Dec;11(12):210182. doi: 10.1098/rsob.210182. Epub 2021 Dec 1. PMID:34847772 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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