Structural determinants in the group III truncated hemoglobin from Campylobacter jejuni (Articolo in rivista)

Type
Label
  • Structural determinants in the group III truncated hemoglobin from Campylobacter jejuni (Articolo in rivista) (literal)
Anno
  • 2006-01-01T00:00:00+01:00 (literal)
Alternative label
  • Nardini, M; Pesce, A; Labarre, M; Richard, C; Bolli, A; Ascenzi, P; Guertin, M; Bolognesi, M (2006)
    Structural determinants in the group III truncated hemoglobin from Campylobacter jejuni
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Nardini, M; Pesce, A; Labarre, M; Richard, C; Bolli, A; Ascenzi, P; Guertin, M; Bolognesi, M (literal)
Pagina inizio
  • 37803 (literal)
Pagina fine
  • 37812 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 281 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Univ Milan, Dept Biomol Sci & Biotechnol, I-20131 Milan, Italy; Univ Milan, CNR, INFM, I-20131 Milan, Italy; Univ Genoa, Dept Phys, CNR, INFM, I-16146 Genoa, Italy; Univ Genoa, Ctr Excellence Biomed Res, I-16146 Genoa, Italy; Univ Laval, Fac Sci & Genie, Dept Biochim & Microbiol, Ste Foy, PQ G1K 7P4, Canada; Univ Roma Tre, Dept Biol, I-00146 Rome, Italy; Univ Roma Tre, Interdept Lab Elect Microscopy, I-00146 Rome, Italy; Natl Inst Infect Dis, IRCCS Lazzaro Spallanzani, I-00149 Rome, Italy (literal)
Titolo
  • Structural determinants in the group III truncated hemoglobin from Campylobacter jejuni (literal)
Abstract
  • Truncated hemoglobins (trHbs) constitute a distinct lineage in the globin superfamily, distantly related in size and fold to myoglobin and monomeric hemoglobins. Their phylogenetic analyses revealed that three groups (I, II, and III) compose the trHb family. Group I and II trHbs adopt a simplified globin fold, essentially composed of a 2-on-2 alpha-helical sandwich, wrapped around the heme group. So far no structural data have been reported for group III trHbs. Here we report the three-dimensional structure of the group III trHbP from the eubacterium Campylobacter jejuni. The 2.15-angstrom resolution crystal structure of C. jejuni trHbP (cyano-met form) shows that the 2-on-2 trHb fold is substantially conserved in the trHb group III, despite the absence of the Gly-based sequence motifs that were considered necessary for the attainment of the trHb specific fold. The heme crevice presents important structural modifications in the C-E region and in the FG helical hinge, with novel surface clefts at the proximal heme site. Contrary to what has been observed for group I and II trHbs, no protein matrix tunnel/cavity system is evident in C. jejuni trHbP. A gating movement of His(E7) side chain (found in two alternate conformations in the crystal structure) may be instrumental for ligand entry to the heme distal site. Sequence conservation allows extrapolating part of the structural results here reported to the whole trHb group III. (literal)
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