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Titolo:
Crystal structure of auracyanin, a "blue" copper protein from the green thermophilic photosynthetic bacterium Chloroflexus aurantiacus
Autore:
Bond, CS; Blankenship, RE; Freeman, HC; Guss, JM; Maher, MJ; Selvaraj, FM; Wilce, MCJ; Willingham, KM;
Indirizzi:
Univ Sydney, Dept Biochem, Sydney, NSW 2006, Australia Univ Sydney SydneyNSW Australia 2006 iochem, Sydney, NSW 2006, Australia Arizona State Univ, Dept Chem & Biochem, Tempe, AZ 85287 USA Arizona StateUniv Tempe AZ USA 85287 Chem & Biochem, Tempe, AZ 85287 USA Univ Sydney, Sch Chem, Sydney, NSW 2006, Australia Univ Sydney Sydney NSWAustralia 2006 h Chem, Sydney, NSW 2006, Australia
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 1, volume: 306, anno: 2001,
pagine: 47 - 67
SICI:
0022-2836(20010209)306:1<47:CSOAA">2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
RESONANCE RAMAN-SPECTRA; CUCUMBER BASIC-PROTEIN; X-RAY-DIFFRACTION; ELECTRON-TRANSFER; ALCALIGENES-DENITRIFICANS; BOUND CYTOCHROME; POPLAR PLASTOCYANIN; ANGSTROM RESOLUTION; REACTION CENTERS; AZURIN;
Keywords:
auracyanin; copper protein; electron transfer; Chloroflexus; photosynthesis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
78
Recensione:
Indirizzi per estratti:
Indirizzo: Freeman, HC Univ Sydney, Dept Biochem, Sydney, NSW 2006, Australia Univ Sydney Sydney NSW Australia 2006 ey, NSW 2006, Australia
Citazione:
C.S. Bond et al., "Crystal structure of auracyanin, a "blue" copper protein from the green thermophilic photosynthetic bacterium Chloroflexus aurantiacus", J MOL BIOL, 306(1), 2001, pp. 47-67

Abstract

Auracyanin B, one of two similar blue copper proteins produced by the thermophilic green non-sulfur photosynthetic bacterium Chloroflexus aurantiacus, crystallizes in space group P6(4)22 (a = b = 115.7 Angstrom, c = 54.6 Angstrom). The structure was solved using multiple wavelength anomalous dispersion data recorded about the CuK absorption edge, and was refined at 1.55 Angstrom resolution. The molecular model comprises 139 amino acid residues, one Cu, 247 H2O molecules, one Cl- and two SO42-. The final residual and estimated standard uncertainties are R = 0.198, ESU = 0.076 Angstrom for atomic coordinates and ESU = 0.05 Angstrom for Cu-ligand bond lengths, respectively. The auracyanin B molecule has a standard cupredoxin fold. With the exception of an additional N-terminal strand, the molecule is very similar tothat of the bacterial cupredoxin, azurin. As in other cupredoxins, one of the Cu ligands lies on strand 4 of the polypeptide, and the other three liealong a large loop between strands 7 and 8. The Cu site geometry is discussed with reference to the amino acid spacing between the latter three ligands. The crystallographically characterized Cu-binding domain of auracyanin B is probably tethered to the periplasmic side of the cytoplasmic membrane by an N-terminal tail that exhibits significant sequence identity with known tethers in several other membrane-associated electron-transfer proteins. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 07:09:06