Structural and functional studies of gpX of escherichia coli phage P2 reveal a widespread role for LysM domains in the baseplates of Contractile-Tailed phages

Journal of Bacteriology

Volumn 195, Issue 24, 2013, Pages 5461-5468

  Maxwell, Karen L ^a   Hassanabad, Mostafa Fatehi ^a   Chang, Tom ^a   Pirani, Nawaz ^a   Bona, Diane ^a   Edwards, Aled M ^a   Davidson, Alan R ^a  

^a UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

DNA; GPX PROTEIN; MALTOSE BINDING PROTEIN; PEPTIDOGLYCAN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ARTICLE; BACTERIOPHAGE P22; BIOINFORMATICS; CONTROLLED STUDY; ELECTRON MICROSCOPY; ESCHERICHIA COLI; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN STRUCTURE;

BACTERIOPHAGE P2; ESCHERICHIA COLI; GLYCOPROTEINS; MAGNETIC RESONANCE SPECTROSCOPY; MICROSCOPY, ELECTRON; PROTEIN CONFORMATION; VIRAL TAIL PROTEINS; VIRION;

EID: 84890209865     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00805-13     Document Type: Article

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