Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion

Proceedings of the National Academy of Sciences of the United States of America

Volumn 104, Issue 30, 2007, Pages 12571-12576

  Yang, Xiaojing ^a   Stojković, Emina A ^a   Kuk, Jane ^a   Moffat, Keith ^a,b  

^a UNIVERSITY OF CHICAGO   (United States)

^b UNIVERSITY OF CHICAGO   (United States)

Author keywords

Biliverdin; Red light photoreceptor

Indexed keywords

ASPARTIC ACID; BACTERIOPHYTOCHROME; BILIVERDIN; PHYTOCHROME; PROTEIN RPBPHP2; PROTEIN RPBPHP3; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; COVALENT BOND; CRYSTAL STRUCTURE; FAR RED LIGHT; LIGHT ABSORPTION; LIGHT HARVESTING SYSTEM; MUTATION; NONHUMAN; PHENOTYPE; PHOTOCHEMISTRY; PHOTOTROPHIC BACTERIUM; PRIORITY JOURNAL; PROTEIN DOMAIN; RED LIGHT; RHODOPSEUDOMONAS PALUSTRIS; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; BILIVERDINE; BINDING SITES; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOTOCHEMISTRY; PHYTOCHROME; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; RHODOBACTER; SEQUENCE ALIGNMENT;

PHOTOBACTERIA; RHODOPSEUDOMONAS PALUSTRIS;

EID: 34547628072     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0701737104     Document Type: Article

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