Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125
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, cyanob...
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ftconicet:oai:ri.conicet.gov.ar:11336/43534 2023-10-09T21:46:03+02:00 Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 Giordano, Daniela Pesce, Alessandra Boechi, Leonardo Bustamante, Juan Pablo Caldelli, Elena Howes, Barry D. Riccio, Alessia di Prisco, Guido Nardini, Marco Estrin, Dario Ariel Smulevich, Giulietta Bolognesi, Martino Verde, Cinzia application/pdf http://hdl.handle.net/11336/43534 eng eng Wiley Blackwell Publishing, Inc info:eu-repo/semantics/altIdentifier/doi/10.1111/febs.13335 info:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/abs/10.1111/febs.13335 http://hdl.handle.net/11336/43534 Giordano, Daniela; Pesce, Alessandra; Boechi, Leonardo; Bustamante, Juan Pablo; Caldelli, Elena; et al.; Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125; Wiley Blackwell Publishing, Inc; Febs Journal; 282; 15; 8-2015; 2948-2965 1742-464X 1742-4658 CONICET Digital CONICET info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ Haloplanktis Extreme Environment Hemeprotein https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 info:eu-repo/semantics/article info:ar-repo/semantics/artículo info:eu-repo/semantics/publishedVersion ftconicet https://doi.org/10.1111/febs.13335 2023-09-24T18:45:55Z 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. Fil: Giordano, Daniela. Consiglio Nazionale delle Ricerche; Italia Fil: Pesce, Alessandra. Università degli Studi di Genova; Italia Fil: Boechi, Leonardo. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Consejo ... Article in Journal/Newspaper Antarc* Antarctic CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Antarctic The Antarctic Argentina Genova ENVELOPE(-82.713,-82.713,-79.863,-79.863) FEBS Journal 282 15 2948 2965 |
institution |
Open Polar |
collection |
CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) |
op_collection_id |
ftconicet |
language |
English |
topic |
Haloplanktis Extreme Environment Hemeprotein https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
spellingShingle |
Haloplanktis Extreme Environment Hemeprotein https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 Giordano, Daniela Pesce, Alessandra Boechi, Leonardo Bustamante, Juan Pablo Caldelli, Elena Howes, Barry D. Riccio, Alessia di Prisco, Guido Nardini, Marco Estrin, Dario Ariel Smulevich, Giulietta Bolognesi, Martino Verde, Cinzia Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 |
topic_facet |
Haloplanktis Extreme Environment Hemeprotein https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
description |
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. Fil: Giordano, Daniela. Consiglio Nazionale delle Ricerche; Italia Fil: Pesce, Alessandra. Università degli Studi di Genova; Italia Fil: Boechi, Leonardo. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Consejo ... |
format |
Article in Journal/Newspaper |
author |
Giordano, Daniela Pesce, Alessandra Boechi, Leonardo Bustamante, Juan Pablo Caldelli, Elena Howes, Barry D. Riccio, Alessia di Prisco, Guido Nardini, Marco Estrin, Dario Ariel Smulevich, Giulietta Bolognesi, Martino Verde, Cinzia |
author_facet |
Giordano, Daniela Pesce, Alessandra Boechi, Leonardo Bustamante, Juan Pablo Caldelli, Elena Howes, Barry D. Riccio, Alessia di Prisco, Guido Nardini, Marco Estrin, Dario Ariel Smulevich, Giulietta Bolognesi, Martino Verde, Cinzia |
author_sort |
Giordano, Daniela |
title |
Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 |
title_short |
Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 |
title_full |
Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 |
title_fullStr |
Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 |
title_full_unstemmed |
Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 |
title_sort |
structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the antarctic marine bacterium pseudoalteromonas haloplanktis tac125 |
publisher |
Wiley Blackwell Publishing, Inc |
url |
http://hdl.handle.net/11336/43534 |
long_lat |
ENVELOPE(-82.713,-82.713,-79.863,-79.863) |
geographic |
Antarctic The Antarctic Argentina Genova |
geographic_facet |
Antarctic The Antarctic Argentina Genova |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/doi/10.1111/febs.13335 info:eu-repo/semantics/altIdentifier/url/https://febs.onlinelibrary.wiley.com/doi/abs/10.1111/febs.13335 http://hdl.handle.net/11336/43534 Giordano, Daniela; Pesce, Alessandra; Boechi, Leonardo; Bustamante, Juan Pablo; Caldelli, Elena; et al.; Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125; Wiley Blackwell Publishing, Inc; Febs Journal; 282; 15; 8-2015; 2948-2965 1742-464X 1742-4658 CONICET Digital CONICET |
op_rights |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
op_doi |
https://doi.org/10.1111/febs.13335 |
container_title |
FEBS Journal |
container_volume |
282 |
container_issue |
15 |
container_start_page |
2948 |
op_container_end_page |
2965 |
_version_ |
1779321703815446528 |