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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Online Access: | http://hdl.handle.net/11567/812422 https://doi.org/10.1111/febs.13335 |
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ftunivgenova:oai:iris.unige.it:11567/812422 2024-04-21T07:46:16+00:00 Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 Giordano, D PESCE, ALESSANDRA Boechi, L Bustamante, JP Caldelli, E Howes, BD Riccio, A di Prisco, G Nardini, M Estrin, D Smulevich, G Bolognesi, M Verde, C. Giordano, D Pesce, Alessandra Boechi, L Bustamante, Jp Caldelli, E Howes, Bd Riccio, A di Prisco, G Nardini, M Estrin, D Smulevich, G Bolognesi, M Verde, C. 2015 ELETTRONICO http://hdl.handle.net/11567/812422 https://doi.org/10.1111/febs.13335 eng eng Wiley info:eu-repo/semantics/altIdentifier/pmid/26040838 info:eu-repo/semantics/altIdentifier/wos/WOS:000358840500011 volume:282 (15) firstpage:2948 lastpage:2965 numberofpages:18 journal:THE FEBS JOURNAL http://hdl.handle.net/11567/812422 doi:10.1111/febs.13335 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84938211607 info:eu-repo/semantics/openAccess info:eu-repo/semantics/article 2015 ftunivgenova https://doi.org/10.1111/febs.13335 2024-03-28T01:17:14Z 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. Article in Journal/Newspaper Antarc* Antarctic Università degli Studi di Genova: CINECA IRIS FEBS Journal 282 15 2948 2965 |
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Open Polar |
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Università degli Studi di Genova: CINECA IRIS |
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ftunivgenova |
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 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. |
author2 |
Giordano, D Pesce, Alessandra Boechi, L Bustamante, Jp Caldelli, E Howes, Bd Riccio, A di Prisco, G Nardini, M Estrin, D Smulevich, G Bolognesi, M Verde, C. |
format |
Article in Journal/Newspaper |
author |
Giordano, D PESCE, ALESSANDRA Boechi, L Bustamante, JP Caldelli, E Howes, BD Riccio, A di Prisco, G Nardini, M Estrin, D Smulevich, G Bolognesi, M Verde, C. |
spellingShingle |
Giordano, D PESCE, ALESSANDRA Boechi, L Bustamante, JP Caldelli, E Howes, BD 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 |
author_facet |
Giordano, D PESCE, ALESSANDRA Boechi, L Bustamante, JP Caldelli, E Howes, BD Riccio, A di Prisco, G Nardini, M Estrin, D Smulevich, G Bolognesi, M Verde, C. |
author_sort |
Giordano, D |
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://hdl.handle.net/11567/812422 https://doi.org/10.1111/febs.13335 |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/26040838 info:eu-repo/semantics/altIdentifier/wos/WOS:000358840500011 volume:282 (15) firstpage:2948 lastpage:2965 numberofpages:18 journal:THE FEBS JOURNAL http://hdl.handle.net/11567/812422 doi:10.1111/febs.13335 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84938211607 |
op_rights |
info:eu-repo/semantics/openAccess |
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 |
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