2ig3

Crystal structure of group III truncated hemoglobin from Campylobacter jejuni

spinqualitylabelsall models 2ig3, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ig3 is a 2 chain structure with sequence from "campylobacter_fetus_subsp._jejuni"_smibert_1974 "campylobacter fetus subsp. jejuni" smibert 1974. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, CYN, HEM, SO4 Related: 1ux8, 1dly, 1dlw, 1idr, 1s69, 1ngk Gene: ctb ("Campylobacter fetus subsp. jejuni" Smibert 1974) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TRHBP_CAMJE] Has been suggested to be involved in cytochrome c peroxidase or P450-like oxygen chemistry or cyanide detoxification. The high oxygen affinity of this protein suggests that it probably does not function as an oxygen transporter. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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-A 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. Structural determinants in the group III truncated hemoglobin from Campylobacter jejuni.,Nardini M, Pesce A, Labarre M, Richard C, Bolli A, Ascenzi P, Guertin M, Bolognesi M J Biol Chem. 2006 Dec 8;281(49):37803-12. Epub 2006 Oct 5. PMID:17023416 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Hemoglobin 3D structures

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