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Titolo:
STRUCTURE OF FERRIC SOYBEAN LEGHEMOGLOBIN-A NICOTINATE AT 2.3-ANGSTROM RESOLUTION
Autore:
ELLIS PJ; APPLEBY CA; GUSS JM; HUNTER WN; OLLIS DL; FREEMAN HC;
Indirizzi:
UNIV SYDNEY,SCH CHEM SYDNEY NSW 2006 AUSTRALIA CSIRO,DIV PLANT IND CANBERRA ACT 2601 AUSTRALIA
Titolo Testata:
Acta crystallographica. Section D, Biological crystallography
, volume: 53, anno: 1997,
parte:, 3
pagine: 302 - 310
SICI:
0907-4449(1997)53:<302:SOFSLN>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
MACROMOLECULAR STRUCTURES; CRYSTAL-STRUCTURE; LIGAND-BINDING; REFINEMENT; MYOGLOBIN; FEATURES; DYNAMICS; LUPIN; HEMOGLOBIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
34
Recensione:
Indirizzi per estratti:
Citazione:
P.J. Ellis et al., "STRUCTURE OF FERRIC SOYBEAN LEGHEMOGLOBIN-A NICOTINATE AT 2.3-ANGSTROM RESOLUTION", Acta crystallographica. Section D, Biological crystallography, 53, 1997, pp. 302-310

Abstract

Soybean leghemoglobin a is a small (16 kDa) protein facilitating the transport of O-2 to respiring N-2-fixing bacteria at low free-O-2 tension. The crystal structure of soybean ferric leghemoglobin a nicotinate has been refined at 2.3 Angstrom resolution. The final R factor is 15.8% for 6877 reflections between 6.0 and 2.3 Angstrom. The structure of soybean leghemoglobin a (143 residues) is closely similar to that of lupin leghemoglobin II (153 residues), the proteins having 82 identical residues when the sequences are aligned. The new structure provides support for the conclusion that the unique properties of leghemoglobin arise principally from a heme pocket considerably larger and more flexible than that of myoglobin, a strongly ruffled heme group, and a proximal histidine orientation more favourable to ligand binding.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 07:28:45