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Titolo:
Mycobacterium tuberculosis hemoglobin N displays a protein tunnel suited for O-2 diffusion to the heme
Autore:
Milani, M; Pesce, A; Ouellet, Y; Ascenzi, P; Guertin, M; Bolognesi, M;
Indirizzi:
Univ Genoa, Dept Phys, INFM, I-16132 Genoa, Italy Univ Genoa Genoa ItalyI-16132 oa, Dept Phys, INFM, I-16132 Genoa, Italy Univ Genoa, Adv Biotechnol Ctr, IST, I-16132 Genoa, Italy Univ Genoa Genoa Italy I-16132 Biotechnol Ctr, IST, I-16132 Genoa, Italy Ist Giannina Gaslini, I-16147 Genoa, Italy Ist Giannina Gaslini Genoa Italy I-16147 a Gaslini, I-16147 Genoa, Italy Univ Rome Tre, Dept Biol, I-00146 Rome, Italy Univ Rome Tre Rome Italy I-00146 ome Tre, Dept Biol, I-00146 Rome, Italy Univ Laval, Fac Sci & Genie, Dept Biochem & Microbiol, Quebec City, PQ G1K7P4, Canada Univ Laval Quebec City PQ Canada G1K 7P4 , Quebec City, PQ G1K7P4, Canada
Titolo Testata:
EMBO JOURNAL
fascicolo: 15, volume: 20, anno: 2001,
pagine: 3902 - 3909
SICI:
0261-4189(20010801)20:15<3902:MTHNDA>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
NITRIC-OXIDE; X-RAY; NITROSATIVE STRESS; CRYSTAL-STRUCTURE; OXYGEN-AFFINITY; LIGAND-BINDING; GLOBIN; FLAVOHEMOGLOBIN; REACTIVITY; MYOGLOBIN;
Keywords:
hemoprotein structure; macrophage oxidative stress; Mycobacterium tuberculosis; nitric oxide; truncated hemoglobins;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Bolognesi, M Univ Genoa, Dept Phys, INFM, Largo Rosanna Benzi 10, I-16132 Genoa, Italy Univ Genoa Largo Rosanna Benzi 10 Genoa Italy I-16132 Italy
Citazione:
M. Milani et al., "Mycobacterium tuberculosis hemoglobin N displays a protein tunnel suited for O-2 diffusion to the heme", EMBO J, 20(15), 2001, pp. 3902-3909

Abstract

Macrophage-generated oxygen- and nitrogen-reactive species control the development of Mycobacterium tuberculosis infection in the host. Mycobacteriumtuberculosis 'truncated hemoglobin' N (trHbN) has been related to nitric oxide (NO) detoxification, in response to macrophage nitrosative stress, during the bacterium latent infection stage. The three-dimensional structure of oxygenated trHbN, solved at 1.9 A resolution, displays the two-over-two alpha -helical sandwich fold recently characterized in two homologous truncated hemoglobins, featuring an extra N-terminal (x-helix and homodimeric assembly. In the absence of a polar distal E7 residue, the O-2 heme ligand is stabilized by two hydrogen bonds to TyrB10(33). Strikingly, ligand diffusion to the heme in trHbN may occur via an apolar tunnel/cavity system extending for similar to 28 Angstrom through the protein matrix, connecting the heme distal cavity to two distinct protein surface sites. This unique structural feature appears to be conserved in several homologous truncated hemoglobins. It is proposed that in trHbN, heme Fe/O-2 stereochemistry and the protein matrix tunnel may promote O-2/NO chemistry in vivo, as a M. tuberculosis defense mechanism against macrophage nitrosative stress.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 23:02:55