Structural characterization of the unligated and choline-bound forms of the major pneumococcal autolysin LytA amidase: Conformational transitions induced by temperature

Journal of Biological Chemistry

Volumn 271, Issue 46, 1996, Pages 29152-29161

  Medrano, Francisco J ^a   Gasset, María ^b   López Zúmel, Consuelo ^b   Usobiaga, Pilar ^b   García, José L ^a   Menéndez, Margarita ^b  

^a CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

^b INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDASE; BACTERIAL ENZYME; CHOLINE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; DIMERIZATION; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME STRUCTURE; ESCHERICHIA COLI; INFRARED SPECTROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; STREPTOCOCCUS PNEUMONIAE;

CHOLINE; CIRCULAR DICHROISM; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE; THERMODYNAMICS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; STREPTOCOCCUS PNEUMONIAE;

EID: 0029831826     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.46.29152     Document Type: Article

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