A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation

Structure

Volumn 8, Issue 11, 2000, Pages 1215-1226

  Symmons, Martyn F ^a   Jones, George H ^b   Luisi, Ben F ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b EMORY UNIVERSITY   (United States)

Author keywords

Degradosome; KH domain; Left handed; S1 domain; Sliding clamp

Indexed keywords

POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN QUATERNARY STRUCTURE; SEQUENCE ANALYSIS; STREPTOMYCES ANTIBIOTICUS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; LIGASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; STREPTOCOCCUS; STRUCTURE-ACTIVITY RELATIONSHIP; TUNGSTEN COMPOUNDS;

EID: 0034435974     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00521-9     Document Type: Article

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