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Titolo:
A noncanonical WD-repeat protein from the cyanobacterium Synechocystis PCC6803: Structural and functional study
Autore:
Hisbergues, M; Gaitatzes, CG; Joset, F; Bedu, S; Smith, TF;
Indirizzi:
CNRS, LCB, F-13402 Marseille 20, France CNRS Marseille France 20CNRS, LCB, F-13402 Marseille 20, France Boston Univ, Coll Engn, Biomol Engn Res Ctr, Boston, MA 02215 USA Boston Univ Boston MA USA 02215 Biomol Engn Res Ctr, Boston, MA 02215 USA Humboldt Univ, Inst Biol, D-10115 Berlin, Germany Humboldt Univ Berlin Germany D-10115 Inst Biol, D-10115 Berlin, Germany
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 2, volume: 10, anno: 2001,
pagine: 293 - 300
SICI:
0961-8368(200102)10:2<293:ANWPFT>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
CRYSTAL-STRUCTURE; CHEY;
Keywords:
WD-repeat protein; structure; inorganic carbon transport; cyanobacteria;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
22
Recensione:
Indirizzi per estratti:
Indirizzo: Joset, F CNRS, LCB, 31 Chemin J Aiguier, F-13402 Marseille 20, France CNRS31 Chemin J Aiguier Marseille France 20 arseille 20, France
Citazione:
M. Hisbergues et al., "A noncanonical WD-repeat protein from the cyanobacterium Synechocystis PCC6803: Structural and functional study", PROTEIN SCI, 10(2), 2001, pp. 293-300

Abstract

Synechocystis PCC6803 possesses several open reading frames encoding putative WD-repeat proteins. One, the Hat protein, is involved in the control ofa high-affinity transport system for inorganic carbon that is active when the cells are grown under a limiting concentration of this carbon substrate. The protein is composed of two major domains separated by a hydrophobic linker region of 20 amino acid residues. The N-terminal domain of Hat has nohomolog in standard databases and does not display any particular structural features. Eleven WD repeats have been identified in the C-terminal moiety. The region encompassing the four terminal WD repeats is essential for growth under a limiting inorganic carbon regime. The region encompassing the two most terminal WD repeats is required for the activity of the high-affinity transport system. However, because the Hat protein is located in the thylakoids, it should not be itself an element of the transport system. The structural organization of the WD-containing domain of Hat was modeled from the crystal structure of the G protein P subunit (with seven WD repeats) and of hemopexin (a structural analog with four blades). Functional and structural data argue in favor of an organization of the Hat WD moiety in two subdomains of seven and four WD repeats. The C-terminal 4-mer subdomain mightinteract with another, yet unknown, protein/peptide. This interaction could be essential in modulating the stability of the 4-mer structure and, thus, the accessibility of this subdomain, or at least of the region encompassing the last two WD repeats.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 05:21:27