Structural and functional studies of H. seropedicae RecA Protein - Insights into the polymerization of RecA protein as nucleoprotein filament

PLoS ONE

Volumn 11, Issue 7, 2016, Pages

  Leite, Wellington C ^a   Galvão, Carolina W ^a   Saab, Sérgio C ^a   Iulek, Jorge ^a   Etto, Rafael M ^a   Steffens, Maria B R ^b   Chitteni Pattu, Sindhu ^c   Stanage, Tyler ^c   Keck, James L ^d   Cox, Michael M ^c  

^a STATE UNIVERSITY OF PONTA GROSSA   (Brazil)

^b FEDERAL UNIVERSITY OF PARANÁ   (Brazil)

^c UNIVERSITY OF WISCONSIN MADISON   (United States)

^d UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ISOLEUCINE; METHIONINE; NUCLEOPROTEIN; PHENYLALANINE; RECA PROTEIN; SINGLE STRANDED DNA; SINGLE STRANDED DNA BINDING PROTEIN; VALINE; BACTERIAL PROTEIN; DNA; PROTEIN BINDING; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DNA STRAND EXCHANGE; ELECTRICAL PARAMETERS; ELECTROSTATIC POTENTIAL; ENZYME ACTIVITY; HERBASPIRILLUM; HERBASPIRILLUM SEROPEDICAE; HYDROGEN BOND; HYDROLYSIS; NONHUMAN; NUCLEIC ACID STRUCTURE, METABOLISM AND FUNCTION; PROTEIN ASSEMBLY; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN POLYMERIZATION; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; STRUCTURE ANALYSIS; TURNOVER NUMBER; CHEMISTRY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR MODEL; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; STATIC ELECTRICITY; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CATALYTIC DOMAIN; DNA; ENZYME ACTIVATION; HERBASPIRILLUM; MODELS, MOLECULAR; NUCLEOPROTEINS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; REC A RECOMBINASES; RECOMBINANT PROTEINS; STATIC ELECTRICITY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 84979699714     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0159871     Document Type: Article

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