Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate

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

Volumn 107, Issue 5, 2010, Pages 1924-1929

  Pazy, Y ^a   Motaleb, M A ^b,c   Guarnieri, M T ^d   Charon, N W ^c   Zhao, R ^d   Silversmith, R E ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b EAST CAROLINA UNIVERSITY   (United States)

^c WEST VIRGINIA UNIVERSITY   (United States)

^d UNIVERSITY OF COLORADO SCHOOL OF MEDICINE   (United States)

Author keywords

CheX; CheY; Convergent evolution; Dephosphorylation; Two component systems

Indexed keywords

PHOSPHATASE; PHOSPHOPROTEIN; PROTEIN CHEX; PROTEIN CHEY3; PROTEIN CHEZ; UNCLASSIFIED DRUG;

ARTICLE; BORRELIA BURGDORFERI; CRYSTAL STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STRUCTURE;

AMINO ACID MOTIFS; BACTERIAL PROTEINS; BORRELIA BURGDORFERI; CATALYTIC DOMAIN; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; EVOLUTION, MOLECULAR; MODELS, MOLECULAR; MULTIPROTEIN COMPLEXES; PHOSPHOPROTEINS; PHOSPHORIC MONOESTER HYDROLASES; PROTEIN CONFORMATION; PROTEIN INTERACTION DOMAINS AND MOTIFS; SIGNAL TRANSDUCTION; SUBSTRATE SPECIFICITY;

BORRELIA BURGDORFERI; ESCHERICHIA COLI; PROKARYOTA;

EID: 76649097688     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0911185107     Document Type: Article

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