3hkx

Crystal structure analysis of an amidase from Nesterenkonia sp.

spinqualitylabelsall models 3hkx, resolution 1.66Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hkx is a 1 chain structure with sequence from Nesterenkonia sp. 10004. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.66Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D0VWZ1_9MICC Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Nesterenkonia strain AN1 was isolated from a screening program for nitrile- and amide-hydrolyzing microorganisms in Antarctic desert soil samples. Strain AN1 showed significant 16S rRNA sequence identity to known members of the genus. Like known Nesterenkonia species, strain AN1 was obligately alkaliphilic (optimum environmental pH, 9 to 10) and halotolerant (optimum environmental Na(+) content, 0 to 15% [wt/vol]) but was also shown to be an obligate psychrophile with optimum growth at approximately 21 degrees C. The partially sequenced genome of AN1 revealed an open reading frame (ORF) encoding a putative protein member of the nitrilase superfamily, referred to as NitN (264 amino acids). The protein crystallized readily as a dimer and the atomic structure of all but 10 amino acids of the protein was determined, confirming that the enzyme had an active site and a fold characteristic of the nitrilase superfamily. The protein was screened for activity against a variety of nitrile, carbamoyl, and amide substrates and was found to have only amidase activity. It had highest affinity for propionamide but demonstrated a low catalytic rate. NitN had maximal activity at 30 degrees C and between pH 6.5 and 7.5, conditions which are outside the optimum growth range for the organism. Unique aliphatic amidase from a psychrotrophic and haloalkaliphilic nesterenkonia isolate.,Nel AJ, Tuffin IM, Sewell BT, Cowan DA Appl Environ Microbiol. 2011 Jun;77(11):3696-702. Epub 2011 Apr 15. PMID:21498772 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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