Structure-based mutagenesis of SigE verifies the importance of hydrophobic and electrostatic residues in type III chaperone function

Molecular Microbiology

Volumn 62, Issue 4, 2006, Pages 928-940

  Knodler, Leigh A ^a   Bertero, Michela ^b,c   Yip, Calvin ^b   Strynadka, Natalie C J ^b   Steele Mortimer, Olivia ^a  

^a NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^c UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; BACTERIAL PROTEIN; CHAPERONE; GLUTAMIC ACID; ISOLEUCINE; LEUCINE; PROTEIN CHAPERONE TYPE 3; PROTEIN SIGD; PROTEIN SIGE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DIMERIZATION; ELECTRICITY; HYDROPHOBICITY; INTRACELLULAR SPACE; LIGHT SCATTERING; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN SECRETION; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TRANSPORT; SALMONELLA ENTERICA; SITE DIRECTED MUTAGENESIS;

BACTERIAL PROTEINS; CRYSTALLOGRAPHY; DIMERIZATION; ELECTROSTATICS; HELA CELLS; HUMANS; HYDROPHOBICITY; MOLECULAR CHAPERONES; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN TRANSPORT; RECOMBINANT PROTEINS; SALMONELLA TYPHIMURIUM; SIGMA FACTOR; STRUCTURE-ACTIVITY RELATIONSHIP;

SALMONELLA; SIGE;

EID: 33750482611     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2006.05418.x     Document Type: Article

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