Artículo

Giordano, D.; Pesce, A.; Boechi, L.; Bustamante, J.P.; Caldelli, E.; Howes, B.D.; Riccio, A.; Di Prisco, G.; Nardini, M.; Estrin, D.; Smulevich, G.; Bolognesi, M.; Verde, C. "Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125" (2015) FEBS Journal. 282(15):2948-2965
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Abstract:

Truncated hemoglobins build one of the three branches of the globin protein superfamily. They display a characteristic two-on-two α-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. The Ph-2/2HbO aquo-met crystal structure (at 2.21 Å resolution) shows typical features of group-II truncated hemoglobins, namely the two-on-two α-helical sandwich fold, a helix Φ 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 probably 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. © 2015 FEBS.

Registro:

Documento: Artículo
Título:Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125
Autor:Giordano, D.; Pesce, A.; Boechi, L.; Bustamante, J.P.; Caldelli, E.; Howes, B.D.; Riccio, A.; Di Prisco, G.; Nardini, M.; Estrin, D.; Smulevich, G.; Bolognesi, M.; Verde, C.
Filiación:Institute of Biosciences and BioResources, National Research Council, Napoli, Italy
Department of Physics, University of Genova, Italy
Departamento de Química Inorgánica, Analítica y Química Física, Universidad de Buenos Aires, Argentina
Department of Chemistry 'Ugo Schiff', University of Firenze, Sesto Fiorentino, Italy
Department of Biosciences, University of Milano, Italy
CNR-Institute of Biophysics and CIMAINA, University of Milano, Italy
Department of Biology, Roma 3 University, Italy
Palabras clave:adaptation; bacterial hemoglobin; molecular dynamics; resonance Raman; X-ray structure; histidine; isoleucine; leucine; methionine; phenylalanine; truncated hemoglobin; tryptophan; tyrosine; heme; hemoglobin; absorption spectroscopy; Article; comparative study; conformational transition; controlled study; crystal structure; electron spin resonance; heme cavity; molecular dynamics; nonhuman; priority journal; protein structure, function and variability; Pseudoalteromonas haloplanktis; Raman spectrometry; structure analysis; structure flexibility; amino acid sequence; Antarctica; chemistry; marine biology; molecular genetics; protein conformation; Pseudoalteromonas; sequence homology; X ray crystallography; Bacteria (microorganisms); Cyanobacteria; Protozoa; Pseudoalteromonas haloplanktis; Amino Acid Sequence; Antarctic Regions; Crystallography, X-Ray; Heme; Hemoglobins; Marine Biology; Molecular Sequence Data; Protein Conformation; Pseudoalteromonas; Sequence Homology, Amino Acid
Año:2015
Volumen:282
Número:15
Página de inicio:2948
Página de fin:2965
DOI: http://dx.doi.org/10.1111/febs.13335
Título revista:FEBS Journal
Título revista abreviado:FEBS J.
ISSN:1742464X
CODEN:FJEOA
CAS:histidine, 645-35-2, 7006-35-1, 71-00-1; isoleucine, 7004-09-3, 73-32-5; leucine, 61-90-5, 7005-03-0; methionine, 59-51-8, 63-68-3, 7005-18-7; phenylalanine, 3617-44-5, 63-91-2; tryptophan, 6912-86-3, 73-22-3; tyrosine, 16870-43-2, 55520-40-6, 60-18-4; heme, 14875-96-8; hemoglobin, 9008-02-0; Heme; Hemoglobins
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_1742464X_v282_n15_p2948_Giordano

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Citas:

---------- APA ----------
Giordano, D., Pesce, A., Boechi, L., Bustamante, J.P., Caldelli, E., Howes, B.D., Riccio, A.,..., Verde, C. (2015) . Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125. FEBS Journal, 282(15), 2948-2965.
http://dx.doi.org/10.1111/febs.13335
---------- CHICAGO ----------
Giordano, D., Pesce, A., Boechi, L., Bustamante, J.P., Caldelli, E., Howes, B.D., et al. "Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125" . FEBS Journal 282, no. 15 (2015) : 2948-2965.
http://dx.doi.org/10.1111/febs.13335
---------- MLA ----------
Giordano, D., Pesce, A., Boechi, L., Bustamante, J.P., Caldelli, E., Howes, B.D., et al. "Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125" . FEBS Journal, vol. 282, no. 15, 2015, pp. 2948-2965.
http://dx.doi.org/10.1111/febs.13335
---------- VANCOUVER ----------
Giordano, D., Pesce, A., Boechi, L., Bustamante, J.P., Caldelli, E., Howes, B.D., et al. Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125. FEBS J. 2015;282(15):2948-2965.
http://dx.doi.org/10.1111/febs.13335