Structure of bacteriophage SPN1S endolysin reveals an unusual two-module fold for the peptidoglycan lytic and binding activity

Molecular Microbiology

Volumn 92, Issue 2, 2014, Pages 316-325

  Park, Yangshin ^a   Lim, Jeong A ^a   Kong, Minsuk ^a   Ryu, Sangryeol ^a,b   Rhee, Sangkee ^a,c  

^a Seoul National University   (South Korea)

^b Seoul National University   (South Korea)

^c Seoul National University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

ENDOLYSIN; GLYCOSIDASE; HYDROLASE; PEPTIDOGLYCAN; UNCLASSIFIED DRUG; PROTEIN BINDING; PROTEINASE;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIOLYSIS; BACTERIOPHAGE; BACTERIUM IDENTIFICATION; BINDING AFFINITY; BINDING SITE; BIOCATALYST; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ESCHERICHIA COLI; FUNCTIONAL ASSESSMENT; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; RESIDUE ANALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; DRUG EFFECTS; ENZYMOLOGY; HYDROLYSIS; METABOLISM; PROTEIN TERTIARY STRUCTURE; SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM; SALMONELLA PHAGE; VIROLOGY; X RAY CRYSTALLOGRAPHY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA; SALMONELLA TYPHIMURIUM;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ENDOPEPTIDASES; ESCHERICHIA COLI; GLYCOSIDE HYDROLASES; HYDROLYSIS; MODELS, MOLECULAR; PEPTIDOGLYCAN; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SALMONELLA PHAGES; SALMONELLA TYPHIMURIUM;

EID: 84897957323     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12555     Document Type: Article

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