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, cyano...
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crwiley:10.1111/febs.13335 2024-09-15T17:42:35+00:00 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 Smulevich, Giulietta Bolognesi, Martino Verde, Cinzia 2015 http://dx.doi.org/10.1111/febs.13335 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Ffebs.13335 https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/febs.13335 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor The FEBS Journal volume 282, issue 15, page 2948-2965 ISSN 1742-464X 1742-4658 journal-article 2015 crwiley https://doi.org/10.1111/febs.13335 2024-07-11T04:38:07Z 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 PSHA a0030 gene from Pseudoalteromonas haloplanktis TAC 125 ( 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) CD 1. 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 O 2 concentration and low kinetic energy of molecules, experienced by organisms living in the Antarctic environment. Database Structural data have been submitted to the Protein Data Bank under accession numbers 4UUR and R4UURSF Article in Journal/Newspaper Antarc* Antarctic Wiley Online Library FEBS Journal 282 15 2948 2965 |
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Open Polar |
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Wiley Online Library |
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crwiley |
language |
English |
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 PSHA a0030 gene from Pseudoalteromonas haloplanktis TAC 125 ( 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) CD 1. 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 O 2 concentration and low kinetic energy of molecules, experienced by organisms living in the Antarctic environment. Database Structural data have been submitted to the Protein Data Bank under accession numbers 4UUR and R4UURSF |
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 Smulevich, Giulietta Bolognesi, Martino Verde, Cinzia |
spellingShingle |
Giordano, Daniela Pesce, Alessandra Boechi, Leonardo Bustamante, Juan Pablo Caldelli, Elena Howes, Barry D. Riccio, Alessia di Prisco, Guido Nardini, Marco Estrin, Dario 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 |
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 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 |
publishDate |
2015 |
url |
http://dx.doi.org/10.1111/febs.13335 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Ffebs.13335 https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/febs.13335 |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
The FEBS Journal volume 282, issue 15, page 2948-2965 ISSN 1742-464X 1742-4658 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/febs.13335 |
container_title |
FEBS Journal |
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282 |
container_issue |
15 |
container_start_page |
2948 |
op_container_end_page |
2965 |
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1810489203795951616 |