Crystal structure of the response regulator spr1814 from Streptococcus pneumoniae reveals unique interdomain contacts among NarL family proteins

Biochemical and Biophysical Research Communications

Volumn 434, Issue 1, 2013, Pages 65-69

  Park, Ae Kyung ^a,c   Moon, Jin Ho ^a   Oh, Jae Soon ^a   Lee, Ki Seog ^b   Chi, Young Min ^a  

^a Korea University   (South Korea)

^b Catholic University of Pusan   (South Korea)

^c NORTHWESTERN UNIVERSITY   (United States)

Author keywords

Helix turn helix fold; NarL subfamily; Response regulators; Streptococcus pneumoniae; Two component phosphotransfer pathways

Indexed keywords

BACTERIAL PROTEIN;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLIZATION; DNA BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN PURIFICATION; STREPTOCOCCUS PNEUMONIAE; TRANSCRIPTION INITIATION;

BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; PHOSPHORYLATION; PROTEIN CONFORMATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; STREPTOCOCCUS PNEUMONIAE;

STREPTOCOCCUS PNEUMONIAE;

EID: 84876808041     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.03.065     Document Type: Article

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