Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily
Autore:
Hopfner, KP; Karcher, A; Shin, DS; Craig, L; Arthur, LM; Carney, JP; Tainer, JA;
Indirizzi:
Scripps Clin & Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 iol, La Jolla, CA 92037 USA Scripps Clin & Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 iol, La Jolla, CA 92037 USA Univ Maryland, Sch Med, Marlene & Stewart Greenebaum Canc Ctr, Dept RadiatOncol,Radiat Oncol Res Lab, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 col Res Lab, Baltimore, MD 21201 USA Univ Maryland, Sch Med, Mol & Cell Biol Grad Program, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 rad Program, Baltimore, MD 21201 USA
Titolo Testata:
CELL
fascicolo: 7, volume: 101, anno: 2000,
pagine: 789 - 800
SICI:
0092-8674(20000623)101:7<789:SBORAA>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
GTPASE-ACTIVATING PROTEINS; NUCLEOTIDE-BINDING FOLD; SACCHAROMYCES-CEREVISIAE; ESCHERICHIA-COLI; HISTIDINE PERMEASE; IONIZING-RADIATION; CRYSTAL-STRUCTURE; CHROMOSOMES SMC; MULTIDRUG-RESISTANCE; TRANSITION-STATE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
73
Recensione:
Indirizzi per estratti:
Indirizzo: Tainer, JA Scripps Clin & Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 la, CA 92037 USA
Citazione:
K.P. Hopfner et al., "Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily", CELL, 101(7), 2000, pp. 789-800

Abstract

To clarify the key role of Rad50 in DNA double-strand break repair (DSBR),we biochemically and structurally characterized ATP-bound and ATP-free Rad50 catalytic domain (Rad50cd) from Pyrococcus furiosus. Rad50cd displays ATPase activity plus ATP-controlled dimerization and DNA binding activities. Rad50cd crystal structures identify probable protein and DNA interfaces andreveal an ABC-ATPase fold, linking Rad50 molecular mechanisms to ABC transporters, including P glycoprotein and cystic fibrosis transmembrane conductance regulator. Binding of ATP gamma-phosphates to conserved signature motifs in two opposing Rad50cd molecules promotes dimerization that likely couples ATP hydrolysis to dimer dissociation and DNA release. These results, validated by mutations, suggest unified molecular mechanisms for ATP-driven cooperativity and allosteric control of ABC-ATPases in DSBR, membrane transport, and chromosome condensation by SMC proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 10:42:19