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Titolo:
H-1, N-15, AND C-13 BACKBONE CHEMICAL-SHIFT ASSIGNMENTS, SECONDARY STRUCTURE, AND MAGNESIUM-BINDING CHARACTERISTICS OF THE BACILLUS-SUBTILIS RESPONSE REGULATOR, SPOOF, DETERMINED BY HETERONUCLEAR HIGH-RESOLUTION NMR
Autore:
FEHER VA; ZAPF JW; HOCH JA; DAHLQUIST FW; WHITELEY JM; CAVANAGH J;
Indirizzi:
UNIV OREGON,INST MOLEC BIOL EUGENE OR 97403 UNIV OREGON,INST MOLEC BIOL EUGENE OR 97403 UNIV OREGON,DEPT CHEM EUGENE OR 97403 SCRIPPS CLIN & RES INST,DEPT MOLEC BIOL LA JOLLA CA 92037 SCRIPPS CLIN & RES INST,DEPT MOLEC & EXPTL MED LA JOLLA CA 92037
Titolo Testata:
Protein science
fascicolo: 9, volume: 4, anno: 1995,
pagine: 1801 - 1814
SICI:
0961-8368(1995)4:9<1801:HNACBC>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-MAGNETIC-RESONANCE; BACTERIAL CHEMOTAXIS; ESCHERICHIA-COLI; LARGER PROTEINS; H-1-NMR SPECTRA; SPECTROSCOPY; CHEY; PROTON; SPORULATION; INTERLEUKIN-1-BETA;
Keywords:
BACTERIAL SIGNAL TRANSDUCTION; CHEY; PHOSPHO-RELAY; 2-COMPONENT SIGNALING SYSTEMS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
54
Recensione:
Indirizzi per estratti:
Citazione:
V.A. Feher et al., "H-1, N-15, AND C-13 BACKBONE CHEMICAL-SHIFT ASSIGNMENTS, SECONDARY STRUCTURE, AND MAGNESIUM-BINDING CHARACTERISTICS OF THE BACILLUS-SUBTILIS RESPONSE REGULATOR, SPOOF, DETERMINED BY HETERONUCLEAR HIGH-RESOLUTION NMR", Protein science, 4(9), 1995, pp. 1801-1814

Abstract

Spo0F, sporulation stage 0 F protein, a 124-residue protein responsible, in part, for regulating the transition of Bacillus subtilis from avegetative state to a dormant endospore, has been studied by high-resolution NMR. The H-1, N-15, and C-13 chemical shift assignments for the backbone residues have been determined from analyses of 3D spectra, N-15 TOCSY-HSQC, N-15 NOESY-HSQC, HNCA, and HN(CO)CA. Assignments for many side-chain proton resonances are also reported. The secondary structure, inferred from short- and medium-range NOEs, (3)J(HN alpha) coupling constants, and hydrogen exchange patterns, define a topology consistent with a doubly wound (alpha/beta)(5) fold. Interestingly, comparison of the secondary structure of Spo0F to the structure of the Escherichia coli response regulator, chemotaxis Y protein (CheY) (Volt K, Matsumura P, 1991, J Biol Chem 266:15511-15519; Bruix M et al., 1993, fur J Biochem 215:573-585), show differences in the relative length ofsecondary structure elements that map onto a single face of the tertiary structure of CheY. This surface may define a region of binding specificity for response regulators. Magnesium titration of Spo0F, followed by amide chemical shift changes, gives an equilibrium dissociation constant of 20 +/- 5 mM. Amide resonances most perturbed by magnesium binding are near the putative site of phosphorylation, Asp 54.

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Documento generato il 03/07/20 alle ore 22:34:58