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Titolo:
The structure of plastocyanin from the cyanobacterium Phormidium laminosum
Autore:
Bond, CS; Bendall, DS; Freeman, HC; Guss, JM; Howe, CJ; Wagner, MJ; Wilce, MCJ;
Indirizzi:
Univ Sydney, Dept Biochem, Sydney, NSW 2006, Australia Univ Sydney SydneyNSW Australia 2006 iochem, Sydney, NSW 2006, Australia Univ Cambridge, Dept Biochem, Cambridge CB2 1QW, England Univ Cambridge Cambridge England CB2 1QW hem, Cambridge CB2 1QW, England Univ Sydney, Sch Chem, Sydney, NSW 2006, Australia Univ Sydney Sydney NSWAustralia 2006 h Chem, Sydney, NSW 2006, Australia Univ Cambridge, Cambridge Ctr Mol Recognit, Cambridge CB2 1QW, England Univ Cambridge Cambridge England CB2 1QW nit, Cambridge CB2 1QW, England
Titolo Testata:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
, volume: 55, anno: 1999,
parte:, 2
pagine: 414 - 421
SICI:
0907-4449(199902)55:<414:TSOPFT>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
RESOLUTION SOLUTION STRUCTURE; CRYSTAL-STRUCTURE; PHOTOSYSTEM-I; GREEN-ALGA; POPLAR PLASTOCYANIN; CYTOCHROME-F; SEQUENCE; EXPRESSION; REFINEMENT; PROGRAM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Bond, CS Univ Sydney, Dept Biochem, Sydney, NSW 2006, Australia Univ Sydney Sydney NSW Australia 2006 ydney, NSW 2006, Australia
Citazione:
C.S. Bond et al., "The structure of plastocyanin from the cyanobacterium Phormidium laminosum", ACT CRYST D, 55, 1999, pp. 414-421

Abstract

The crystal structure of the 'blue' copper protein plastocyanin from the cyanobacterium Phormidium laminosum has been solved and refined using 2.8 Angstrom X-ray data. P. laminosum, plastocyanin crystallizes in space group P4(3)2(1)2 with unit-cell dimensions a =86.57, c = 91.47 Angstrom and with three protein molecules per asymmetric unit. The final residual R is 19.9%. The structure was solved using molecular replacement with a search model based on the crystal structure of a close homologue? Anabaena variabilis plastocyanin (66% sequence identity). The molecule of P. laminosum plastocyaninhas 105 amino-acid residues. The single Cu atom is coordinated by the sameresidues-two histidines, a cysteine and a methionine as in other plastocyanins. In the crystal structure, the three molecules of the asymmetric unit are related by a noncrystallographic threefold axis. A Zn atom lies betweeneach pair of neighbouring molecules in this ensemble, being coordinated bya surface histidine residue of one molecule and by two aspartates of the other.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/11/20 alle ore 19:43:32