The structure of an unconventional HD-GYP protein from bdellovibrio reveals the roles of conserved residues in this class of Cyclic-di-GMP phosphodiesterases

mBio

Volumn 2, Issue 5, 2011, Pages

  Lovering, Andrew L ^a   Capeness, Michael J ^b   Lambert, Carey ^b   Hobley, Laura ^b   Sockett, R Elizabeth ^b  

^a UNIVERSITY OF BIRMINGHAM   (United Kingdom)

^b UNIVERSITY OF NOTTINGHAM   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYCLIC GMP PHOSPHODIESTERASE; HD GYP PROTEIN; HYDROXIDE; PHOSPHATE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BDELLOVIBRIO; BINDING SITE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN MOTIF; PROTEIN STRUCTURE; REGULATORY MECHANISM; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS;

BACTERIA (MICROORGANISMS); BDELLOVIBRIO; BDELLOVIBRIO BACTERIOVORUS;

EID: 80455158430     PISSN: None     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00163-11     Document Type: Article

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