4uur | pdb_00004uur

Cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125

spinqualitylabelsall models 4uur, resolution 2.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4uur is a 2 chain structure with sequence from Pseudoalteromonas haloplanktis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.21Å Ligands: HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3IDI7_PSET1 Publication Abstract from PubMed Truncated hemoglobins build one of the three branches of the globin protein superfamily. They display a characteristic two-on-two alpha-helical sandwich fold and are clustered into three groups (I, II, and III) based on distinct structural features. Truncated hemoglobins are present in eubacteria, cyanobacteria, protozoa and plants. Here we present a structural, spectroscopic and molecular dynamics characterization of a group-II truncated hemoglobin, encoded by the PSHAa0030 gene from Pseudoalteromonas haloplanktis TAC125 (Ph-2/2HbO), a cold-adapted Antarctic marine bacterium hosting one flavohemoglobin and three distinct truncated hemoglobins. Ph-2/2HbO aquo-met crystal structure (at 2.21 A resolution) shows typical features of group-II truncated hemoglobins, namely the two-on-two alpha-helical sandwich fold, a helix Phi preceding the proximal helix F, and a heme distal-site hydrogen bonded network that includes water molecules and several distal-site residues, including His(58)CD1. Analysis of Ph-2/2HbO by electron paramagnetic resonance, resonance Raman and electronic absorption spectra, under varied solution conditions, shows that Ph-2/2HbO can access diverse heme ligation states. Among these, detection of a low-spin heme hexa-coordinated species suggests that residue Tyr(42)B10 can undergo large conformational changes in order to act as the sixth heme-Fe ligand. Altogether, the results show that Ph-2/2HbO maintains the general structural features of group-II truncated hemoglobins, but displays enhanced conformational flexibility in the proximity of the heme cavity, a property likely related to the functional challenges, such as low temperature, high O2 concentration and low kinetic energy of molecules, experienced by organisms living in the Antarctic environment. This article is protected by copyright. All rights reserved. Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125.,Giordano D, Pesce A, Boechi L, Bustamante JP, Caldelli E, Howes BD, Riccio A, di Prisco G, Nardini M, Estrin D, Smulevich G, Bolognesi M, Verde C FEBS J. 2015 Jun 4. doi: 10.1111/febs.13335. PMID:26040838 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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