4ao7

Zinc bound structure of a novel cold-adapted esterase from an Arctic intertidal metagenomic library

spinqualitylabelsall models 4ao7, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ao7 is a 1 chain structure with sequence from Unidentified. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed A novel cold-adapted lipolytic enzyme gene, est97, was identified from a high Arctic intertidal zone sediment metagenomic library. The deduced amino acid sequence of Est97 showed low similarity with other lipolytic enzymes, the maximum being 30 % identity with a putative lipase from Vibrio caribbenthicus. Common features of lipolytic enzymes, such as the GXSXG sequence motif, were detected. The gene product was over-expressed in Escherichia coli and purified. The recombinant Est97 (rEst97) hydrolysed various rho-nitrophenyl esters with the best substrate being rho-nitrophenyl hexanoate (K (m) and k (cat) of 39 muM and 25.8 s(-1), respectively). This esterase activity of rEst97 was optimal at 35 degrees C and pH 7.5 and the enzyme was unstable at temperatures above 25 degrees C. The apparent melting temperature, as determined by differential scanning calorimetry was 39 degrees C, substantiating Est97 as a cold-adapted esterase. The crystal structure of rEst97 was determined by the single wavelength anomalous dispersion method to 1.6 A resolution. The protein was found to have a typical alpha/beta-hydrolase fold with Ser144-His226-Asp197 as the catalytic triad. A suggested, relatively short lid domain of rEst97 is composed of residues 80-114, which form an alpha-helix and a disordered loop. The cold adaptation features seem primarily related to a high number of methionine and glycine residues and flexible loops in the high-resolution structures. Functional and structural studies of a novel cold-adapted esterase from an Arctic intertidal metagenomic library.,Fu J, Leiros HK, de Pascale D, Johnson KA, Blencke HM, Landfald B Appl Microbiol Biotechnol. 2012 Jul 26. PMID:22832985 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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