The structural role of the zinc ion can be dispensable in prokaryotic zinc-finger domains

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

Volumn 106, Issue 17, 2009, Pages 6933-6938

  Baglivo, Ilaria ^a   Russo, Luigi ^a   Esposito, Sabrina ^a   Malgieri, Gaetano ^a   Renda, Mario ^a   Salluzzo, Antonio ^b   Di Blasio, Benedetto ^a   Isernia, Carla ^a   Fattorusso, Roberto ^a   Pedone, Paolo V ^a  

^a SECOND UNIVERSITY OF NAPLES   (Italy)

^b ENEA   (Italy)

Author keywords

Cys2His2 zinc finger; DNA binding proteins; Metal binding proteins; Ros protein

Indexed keywords

ASPARTIC ACID; CYSTEINE; PROTEIN DERIVATIVE; ROS PROTEIN; UNCLASSIFIED DRUG; ZINC ION; BACTERIAL PROTEIN; CATION; ZINC; ZINC FINGER PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; DATA BASE; DNA BINDING; EUKARYOTE; GENE TRANSFER; MESORHIZOBIUM; MESORHIZOBIUM LOTI; MUTANT; NONHUMAN; NUCLEOTIDE SEQUENCE; POINT MUTATION; PRIORITY JOURNAL; PROKARYOTE; STRUCTURE ANALYSIS; ZINC FINGER MOTIF; ALPHAPROTEOBACTERIA; AMINO ACID SEQUENCE; CHEMISTRY; GENETICS; HYDROPHOBICITY; MASS SPECTROMETRY; METABOLISM; MOLECULAR GENETICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY;

AGROBACTERIUM; EUKARYOTA; PROKARYOTA;

ALPHAPROTEOBACTERIA; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CATIONS; HYDROPHOBICITY; MASS SPECTROMETRY; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; ZINC; ZINC FINGERS;

EID: 66349098084     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0810003106     Document Type: Article

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