期刊论文详细信息
FEBS Letters
Location of enzymatic and DNA‐binding domains on E. coli protease La
Baker, Michael E.1 
[1] Department of Medicine, M-023, University of California, San Diego, La Jolla, CA 92093, USA
关键词: Protease La;    ATP-dependent protease;    DNA-binding protease;   
DOI  :  10.1016/0014-5793(89)81155-X
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

Escherichia coli protease La is an ATP-dependent enzyme that has a DNA-binding site. The locations of the enzymatic and DNA-binding sites are not known. We report that a 75-residue segment at the carboxy-terminus of the protease La is similar to part of Bacillus licheniformis β-lactamase, a serine enzyme. The comparison score is 8.2 standard deviations higher than that obtained with 10 000 comparisons of randomized sequences of these segments. The probability of obtaining such a score by chance is 1.2 × 10−16. We also find that a 107-residue segment in the amino-terminus half of protease La is similar to part of the sopB protein, a DNA-binding protein of the plasmid F of E. coli. The comparison score for these segments is 8 standard deviations (P = 6 × 10−16). These strong amino acid sequence similarities suggest the locations of the catalytic serine and the DNA-binding domains of protease La.

【 授权许可】

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