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Titolo:
Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution
Autore:
Bertelsen, EB; Zhou, HJ; Lowry, DF; Flynn, GC; Dahlquist, FW;
Indirizzi:
Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA Univ Oregon Eugene OR USA 97403 egon, Inst Mol Biol, Eugene, OR 97403 USA NCI,,Macromol NMR Sect, ABL Basic Res Program, Frederick Canc Res & Dev Ctr NCI Ft Detrick MD USA 21702 sic Res Program, Frederick Canc Res & Dev Ctr Battelle2Mem Inst, Pacific NW Labs, Environm Mol Sci Lab, Richland, WA 9935 Battelle Mem Inst Richland WA USA 99352 nm Mol Sci Lab, Richland, WA 9935
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 2, volume: 8, anno: 1999,
pagine: 343 - 354
SICI:
0961-8368(199902)8:2<343:TADOT1>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI DNAJ; ROTATIONAL DIFFUSION ANISOTROPY; NMR STRUCTURE DETERMINATION; NUCLEAR-MAGNETIC-RESONANCE; MOLECULAR CHAPERONE DNAK; PEPTIDE-BINDING DOMAIN; SHOCK COGNATE PROTEIN; SIDE-CHAIN RESONANCES; BACKBONE DYNAMICS; SUBSTRATE-BINDING;
Keywords:
DnaK; molecular chaperone; NMR; N-15 relaxation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
70
Recensione:
Indirizzi per estratti:
Indirizzo: Dahlquist, FW Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA Univ Oregon Eugene OR USA 97403 Biol, Eugene, OR 97403 USA
Citazione:
E.B. Bertelsen et al., "Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution", PROTEIN SCI, 8(2), 1999, pp. 343-354

Abstract

Hsp70 molecular chaperones contain three distinct structural domains, a 44kDa N-terminal ATPase domain, a 17 kDa peptide-binding domain, and a 10 kDa C-terminal domain. The ATPase and peptide binding domains are conserved in sequence and are functionally well characterized. The function of the 10 kDa variable C-terminal domain is less well understood. We have characterized the secondary structure and dynamics of the C-terminal domain from the Escherichia coli Hsp70, DnaK, in solution by high-resolution NMR. The domainwas shown to be comprised of a rigid structure consisting of four helices and a flexible C-terminal subdomain of approximately 33 amino acids. The mobility of the flexible region is maintained in the context of the full-length protein and does not appear to be modulated by the nucleotide state. Theflexibility of this region appears to be a conserved feature of Hsp70 architecture and may have important functional implications. We also developed a method to analyze N-15 nuclear spin relaxation data, which allows us to extract amide bond vector directions relative to a unique diffusion axis. The extracted angles and rotational correlation times indicate that the helices form an elongated, bundle-like structure in solution.

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Documento generato il 09/07/20 alle ore 01:36:26