Determination of the self-association residues within a homomeric and a heteromeric AAA + enhancer binding protein

Journal of Molecular Biology

Volumn 426, Issue 8, 2014, Pages 1692-1710

  Lawton, Edward ^a   Jovanovic, Milija ^a   Joly, Nicolas ^b   Waite, Christopher ^a   Zhang, Nan ^a   Wang, Baojun ^c   Burrows, Patricia ^a   Buck, Martin ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

^b INSTITUT JACQUES MONOD   (France)

^c UNIVERSITY OF EDINBURGH   (United Kingdom)

Author keywords

HrpR; HrpS; Pseudomonas syringae; PspF

Indexed keywords

ADENOSINE TRIPHOSPHATASE ASSOCIATED WITH VARIOUS CELLULAR ACTIVITIES ENHANCER BINDING PROTEIN; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; BINDING PROTEIN; MUTANT PROTEIN; PROTEIN HRPR; PROTEIN HRPS; PROTEIN HRPV; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; AQUIFEX AEOLICUS; ARTICLE; AZOTOBACTER VINELANDII; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ESCHERICHIA COLI; MUTAGENESIS; NONHUMAN; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PSEUDOMONAS; PSEUDOMONAS PUTIDA; PSEUDOMONAS SYRINGAE; RHODOBACTER SPHAEROIDES; SALMONELLA ENTERICA; SALMONELLA TYPHIMURIUM; SEQUENCE ALIGNMENT; SINORHIZOBIUM MELILOTI; TRANSCRIPTION INITIATION; WASTE;

BACTERIA (MICROORGANISMS); PSEUDOMONAS SYRINGAE;

ABBREVIATIONS; BACTERIAL ENHANCER BINDING PROTEIN; BACTERIAL TWO-HYBRID; BACTH; BEBP; HRPR; HRPS; PSEUDOMONAS SYRINGAE; PSPF; RNA POLYMERASE; RNAP; Σ(54);

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; DNA-BINDING PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROMOTER REGIONS, GENETIC; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; PSEUDOMONAS SYRINGAE; RECOMBINANT PROTEINS; RNA POLYMERASE SIGMA 54; SEQUENCE HOMOLOGY, AMINO ACID; TRANSCRIPTION FACTORS;

EID: 84897116483     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.01.001     Document Type: Article

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