Involvement of the N Domain Residues E34, K35, and R38 in the Functionally Active Structure of Escherichia coli Lon Protease.

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作者： A G,Andrianova ^[1] ; A M,Kudzhaev ^[1] ; V A,Abrikosova ^[1] ; A E,Gustchina ^[2] ; I V,Smirnov ^[1] ; T V,Rotanova ^[1]

作者单位： Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997 Russia. ^[1] Macromolecular Crystallography Laboratory, NCI-Frederick, P.O. Box B, Frederick, MD 21702, USA. ^[2]

关键词 AAA+ proteins ATP-dependent proteolysis LonA proteases N domain cellular proteome quality control

DOI 10.32607/actanaturae.11197

PMID 33456980

发布时间 2023-11-10

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Involvement of the N Domain Residues E34, K35, and R38 in the Functionally Active Structure of Escherichia coli Lon Protease.

Acta naturae

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Acta naturae

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Involvement of the N Domain Residues E34, K35, and R38 in the Functionally Active Structure of Escherichia coli Lon Protease.

Acta naturae

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Acta naturae

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