Proteolysis of truncated hemolysin A yields a stable dimerization interface.

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作者： Walter R P,Novak ^[1] ; Basudeb,Bhattacharyya ^[2] ; Daniel P,Grilley ^[2] ; Todd M,Weaver ^[2]

作者单位： Department of Chemistry, Wabash College, 301 West Wabash Avenue, Crawfordsville, IN 47933, USA. ^[1] Department of Chemistry and Biochemistry, University of Wisconsin-La Crosse, 1725 State Street, La Crosse, WI 54601, USA. ^[2]

关键词 Proteus mirabilis alternate crystal forms hemolysin A proteolysis two-partner secretion β-helix

主题词氨基酸序列(Amino Acid Sequence);细菌蛋白质类(Bacterial Proteins);结合部位(Binding Sites);克隆, 分子(Cloning, Molecular);结晶学, X线(Crystallography, X-Ray);大肠杆菌(Escherichia coli);基因表达(Gene Expression);溶血素蛋白质类(Hemolysin Proteins);氢键合(Hydrogen Bonding);模型, 分子(Models, Molecular);突变(Mutation);质粒(Plasmids);蛋白质结合(Protein Binding);蛋白质相互作用域和基序(Protein Interaction Domains and Motifs);蛋白质多聚化(Protein Multimerization);蛋白质结构, 四级(Protein Structure, Quaternary);蛋白质结构, 三级(Protein Structure, Tertiary);奇异变形杆菌(Proteus mirabilis);重组蛋白质类(Recombinant Proteins)

DOI 10.1107/S2053230X17002102

PMID 28291749

发布时间 2024-05-24

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Acta crystallographica. Section F, Structural biology communications

2017年73卷Pt 3期

138-145页

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Proteolysis of truncated hemolysin A yields a stable dimerization interface.

Acta crystallographica. Section F, Structural biology communications

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Acta crystallographica. Section F, Structural biology communications

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Proteolysis of truncated hemolysin A yields a stable dimerization interface.

Acta crystallographica. Section F, Structural biology communications

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Acta crystallographica. Section F, Structural biology communications

相关期刊

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