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Titolo:
THE STRUCTURE OF A PHYTOCYANIN, THE BASIC BLUE PROTEIN FROM CUCUMBER,REFINED AT 1.8 ANGSTROM RESOLUTION
Autore:
GUSS JM; MERRITT EA; PHIZACKERLEY RP; FREEMAN HC;
Indirizzi:
UNIV SYDNEY,DEPT BIOCHEM SYDNEY NSW 2006 AUSTRALIA UNIV SYDNEY,SCH CHEM SYDNEY NSW 2006 AUSTRALIA STANFORD SYNCHROTRON RADIAT LAB STANFORD CA 94039
Titolo Testata:
Journal of Molecular Biology
fascicolo: 5, volume: 262, anno: 1996,
pagine: 686 - 705
SICI:
0022-2836(1996)262:5<686:TSOAPT>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRYSTAL-STRUCTURE ANALYSIS; ALCALIGENES-FAECALIS S-6; AMINO-ACID-SEQUENCE; LEAST-SQUARES REFINEMENT; COPPER-BINDING PROTEINS; ELECTRON-TRANSFER; ACTIVE-SITE; MACROMOLECULAR STRUCTURES; POPLAR PLASTOCYANIN; PHASE DETERMINATION;
Keywords:
CUCUMBER BASIC PROTEIN; BLUE COPPER PROTEIN; CUPREDOXIN; PHYTOCYANIN; MAD PHASING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
76
Recensione:
Indirizzi per estratti:
Citazione:
J.M. Guss et al., "THE STRUCTURE OF A PHYTOCYANIN, THE BASIC BLUE PROTEIN FROM CUCUMBER,REFINED AT 1.8 ANGSTROM RESOLUTION", Journal of Molecular Biology, 262(5), 1996, pp. 686-705

Abstract

The crystal structure of the cucumber basic protein (CBP), a type 1 or blue copper protein, has been refined at 1.8 Angstrom resolution. The molecule resembles other blue copper proteins in having a Greek key beta-barrel structure, except that the barrel is open on one side and is better described as a ''beta-sandwich'' or ''beta-taco''. The Cu atom has the normal blue copper NNSS' co-ordination with bond lengths Cu-N(His39) = 1.93 Angstrom, Cu-S(Cys79) = 2.16 Angstrom, Cu-N(His84) = 1.95 Angstrom, Cu-S(Met89) = 2.61 Angstrom. The Cu-S(Met) bond is the shortest so far observed in a blue copper protein. A disulphide link, (Cys52)-S-S-(Cys85), appears to play an important role in stabilising the molecular structure. It is suggested that the polypeptide fold is typical of a sub-family of blue copper proteins (phytocyanins) as wellas a non-metalloprotein, ragweed allergen Ra3, with which CBP has a high degree of sequence identity. The proteins currently identifiable as phytocyanins are CBP, stellacyanin, mavicyanin, umecyanin, a cucumber peeling cupredoxin, a putative blue copper protein in pea pads, and a blue copper protein from Arabidopsis thaliana, In all except CBP andthe pea-pod protein, the axial methionine Ligand normally found at blue copper sites is replaced by glutamine. The structure of CBP was originally solved by the multiple wavelength anomalous scattering method,using data recorded at four wavelengths. All these data were includedin the restrained least squares refinement. The final model comprises96 amino acid residues, 122 solvent molecules and a copper atom. Several residues are modelled as having more than one conformation. The residual R is 0.141 for 41,910 observations (including Bijvoet-related observations) of 8.142 unique reflections in the resolution range 7 to 1.8 Angstrom. (C) 1996 Academic Press Limited

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 08:16:57