3HKX

Crystal structure analysis of an amidase from Nesterenkonia sp.

3HKX の概要

• エントリーDOI: 10.2210/pdb3hkx/pdb
• 分子名称: Amidase (2 entities in total)
• 機能のキーワード: alpha-beta-beta-alpha:alpha-beta-beta-alpha dimeric sandwich, hydrolase
• 由来する生物種: Nesterenkonia sp. 10004
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30116.79

構造登録者

Sewell, B.T.,Nel, A.J.M.,Cowan, D.A. (登録日: 2009-05-26, 公開日: 2009-06-09, 最終更新日: 2023-09-06)

主引用文献

Nel, A.J.,Tuffin, I.M.,Sewell, B.T.,Cowan, D.A.
Unique aliphatic amidase from a psychrotrophic and haloalkaliphilic nesterenkonia isolate.
Appl.Environ.Microbiol., 77:3696-3702, 2011

PubMed Abstract: 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°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°C and between pH 6.5 and 7.5, conditions which are outside the optimum growth range for the organism.

PubMed: 21498772
DOI: 10.1128/AEM.02726-10

実験手法

X-RAY DIFFRACTION (1.66 Å)