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/2434/342532 https://doi.org/10.1111/febs.13335 |
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ftunivmilanoair:oai:air.unimi.it:2434/342532 2024-04-21T07:49:54+00:00 Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 D. Giordano A. Pesce L. Boechi J. P. Bustamante E. Caldelli B. D. Howes A. Riccio G. Di Prisco D. Estrin G. Smulevich C. Verde M. Nardini M. Bolognesi D. Giordano A. Pesce L. Boechi J.P. Bustamante E. Caldelli B.D. Howe A. Riccio G. Di Prisco M. Nardini D. Estrin G. Smulevich M. Bolognesi C. Verde 2015-08 http://hdl.handle.net/2434/342532 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 issue:15 firstpage:2948 lastpage:2965 numberofpages:18 journal:THE FEBS JOURNAL http://hdl.handle.net/2434/342532 doi:10.1111/febs.13335 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84938211607 info:eu-repo/semantics/closedAccess adaptation bacterial hemoglobin molecular dynamic resonance Raman X-ray structure Amino Acid Sequence Antarctic Region Crystallography X-Ray Heme Hemoglobin Molecular Sequence Data Protein Conformation Pseudoalteromona Sequence Homology Amino Acid Marine Biology Biochemistry Cell Biology Molecular Biology Medicine (all) Settore BIO/10 - Biochimica Settore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin) info:eu-repo/semantics/article 2015 ftunivmilanoair https://doi.org/10.1111/febs.13335 2024-03-27T16:39:24Z 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 The University of Milan: Archivio Istituzionale della Ricerca (AIR) FEBS Journal 282 15 2948 2965 |
institution |
Open Polar |
collection |
The University of Milan: Archivio Istituzionale della Ricerca (AIR) |
op_collection_id |
ftunivmilanoair |
language |
English |
topic |
adaptation bacterial hemoglobin molecular dynamic resonance Raman X-ray structure Amino Acid Sequence Antarctic Region Crystallography X-Ray Heme Hemoglobin Molecular Sequence Data Protein Conformation Pseudoalteromona Sequence Homology Amino Acid Marine Biology Biochemistry Cell Biology Molecular Biology Medicine (all) Settore BIO/10 - Biochimica Settore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin) |
spellingShingle |
adaptation bacterial hemoglobin molecular dynamic resonance Raman X-ray structure Amino Acid Sequence Antarctic Region Crystallography X-Ray Heme Hemoglobin Molecular Sequence Data Protein Conformation Pseudoalteromona Sequence Homology Amino Acid Marine Biology Biochemistry Cell Biology Molecular Biology Medicine (all) Settore BIO/10 - Biochimica Settore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin) D. Giordano A. Pesce L. Boechi J. P. Bustamante E. Caldelli B. D. Howes A. Riccio G. Di Prisco D. Estrin G. Smulevich C. Verde M. Nardini M. Bolognesi Structural flexibility of the heme cavity in the cold-adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 |
topic_facet |
adaptation bacterial hemoglobin molecular dynamic resonance Raman X-ray structure Amino Acid Sequence Antarctic Region Crystallography X-Ray Heme Hemoglobin Molecular Sequence Data Protein Conformation Pseudoalteromona Sequence Homology Amino Acid Marine Biology Biochemistry Cell Biology Molecular Biology Medicine (all) Settore BIO/10 - Biochimica Settore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin) |
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 |
D. Giordano A. Pesce L. Boechi J.P. Bustamante E. Caldelli B.D. Howe A. Riccio G. Di Prisco M. Nardini D. Estrin G. Smulevich M. Bolognesi C. Verde |
format |
Article in Journal/Newspaper |
author |
D. Giordano A. Pesce L. Boechi J. P. Bustamante E. Caldelli B. D. Howes A. Riccio G. Di Prisco D. Estrin G. Smulevich C. Verde M. Nardini M. Bolognesi |
author_facet |
D. Giordano A. Pesce L. Boechi J. P. Bustamante E. Caldelli B. D. Howes A. Riccio G. Di Prisco D. Estrin G. Smulevich C. Verde M. Nardini M. Bolognesi |
author_sort |
D. Giordano |
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/2434/342532 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 issue:15 firstpage:2948 lastpage:2965 numberofpages:18 journal:THE FEBS JOURNAL http://hdl.handle.net/2434/342532 doi:10.1111/febs.13335 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84938211607 |
op_rights |
info:eu-repo/semantics/closedAccess |
op_doi |
https://doi.org/10.1111/febs.13335 |
container_title |
FEBS Journal |
container_volume |
282 |
container_issue |
15 |
container_start_page |
2948 |
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2965 |
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