Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain
The structure of the BA42 protein belonging to the Antarctic flavobacterium Bizionia argentinensis was determined by nuclear magnetic resonance and X-ray crystallography. This is the first structure of a member of the PF04536 family comprised of a stand-alone TPM domain. The structure reveals a new...
Published in: | Proteins: Structure, Function, and Bioinformatics |
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Main Authors: | , , , , , , , , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
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Wiley
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Online Access: | http://hdl.handle.net/11336/8535 |
_version_ | 1821771714730655744 |
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author | Aran, Martin Smal, Clara Pelliza, Leonardo Gallo, Mariana Otero, Lisandro Horacio Klinke, Sebastian Goldbaum, Fernando Alberto Ithurralde, Esteban Bercovich, Andrés Mac Cormack, Walter P. Turjanski, Adrian G. Cicero, Daniel Oscar |
author_facet | Aran, Martin Smal, Clara Pelliza, Leonardo Gallo, Mariana Otero, Lisandro Horacio Klinke, Sebastian Goldbaum, Fernando Alberto Ithurralde, Esteban Bercovich, Andrés Mac Cormack, Walter P. Turjanski, Adrian G. Cicero, Daniel Oscar |
author_sort | Aran, Martin |
collection | CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) |
container_issue | 11 |
container_start_page | 3062 |
container_title | Proteins: Structure, Function, and Bioinformatics |
container_volume | 82 |
description | The structure of the BA42 protein belonging to the Antarctic flavobacterium Bizionia argentinensis was determined by nuclear magnetic resonance and X-ray crystallography. This is the first structure of a member of the PF04536 family comprised of a stand-alone TPM domain. The structure reveals a new topological variant of the four β-strands constituting the central β-sheet of the αβα architecture and a double metal binding site stabilizing a pair of crossing loops, not observed in previous structures of proteins belonging to this family. BA42 shows differences in structure and dynamics in the presence or absence of bound metals. The affinity for divalent metal ions is close to that observed in proteins that modulate their activity as a function of metal concentration, anticipating a possible role for BA42. Fil: Aran, Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina Fil: Smal, Clara. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina Fil: Pelliza, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina Fil: Gallo, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina Fil: Otero, Lisandro Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Plataforma Argentina ... |
format | Article in Journal/Newspaper |
genre | Antarc* Antarctic |
genre_facet | Antarc* Antarctic |
geographic | Antarctic The Antarctic Argentina |
geographic_facet | Antarctic The Antarctic Argentina |
id | ftconicet:oai:ri.conicet.gov.ar:11336/8535 |
institution | Open Polar |
language | English |
op_collection_id | ftconicet |
op_container_end_page | 3078 |
op_doi | https://doi.org/10.1002/prot.24667 |
op_relation | info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/prot.24667/abstract info:eu-repo/semantics/altIdentifier/doi/10.1002/prot.24667 http://hdl.handle.net/11336/8535 |
op_rights | info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
publisher | Wiley |
record_format | openpolar |
spelling | ftconicet:oai:ri.conicet.gov.ar:11336/8535 2025-01-16T19:38:30+00:00 Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain Aran, Martin Smal, Clara Pelliza, Leonardo Gallo, Mariana Otero, Lisandro Horacio Klinke, Sebastian Goldbaum, Fernando Alberto Ithurralde, Esteban Bercovich, Andrés Mac Cormack, Walter P. Turjanski, Adrian G. Cicero, Daniel Oscar application/pdf http://hdl.handle.net/11336/8535 eng eng Wiley info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/prot.24667/abstract info:eu-repo/semantics/altIdentifier/doi/10.1002/prot.24667 http://hdl.handle.net/11336/8535 info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ Structural Genomics Antarctic Bacteria Bizionia Argentinensis Ba42 Protein Structure Nuclear Magnetic Resonance X-Ray Crystallography https://purl.org/becyt/ford/1.6 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/10.1002/prot.24667 2024-10-04T09:34:04Z The structure of the BA42 protein belonging to the Antarctic flavobacterium Bizionia argentinensis was determined by nuclear magnetic resonance and X-ray crystallography. This is the first structure of a member of the PF04536 family comprised of a stand-alone TPM domain. The structure reveals a new topological variant of the four β-strands constituting the central β-sheet of the αβα architecture and a double metal binding site stabilizing a pair of crossing loops, not observed in previous structures of proteins belonging to this family. BA42 shows differences in structure and dynamics in the presence or absence of bound metals. The affinity for divalent metal ions is close to that observed in proteins that modulate their activity as a function of metal concentration, anticipating a possible role for BA42. Fil: Aran, Martin. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina Fil: Smal, Clara. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina Fil: Pelliza, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina Fil: Gallo, Mariana. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Fundación Instituto Leloir; Argentina Fil: Otero, Lisandro Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquimicas de Buenos Aires; Argentina. Plataforma Argentina ... Article in Journal/Newspaper Antarc* Antarctic CONICET Digital (Consejo Nacional de Investigaciones Científicas y Técnicas) Antarctic The Antarctic Argentina Proteins: Structure, Function, and Bioinformatics 82 11 3062 3078 |
spellingShingle | Structural Genomics Antarctic Bacteria Bizionia Argentinensis Ba42 Protein Structure Nuclear Magnetic Resonance X-Ray Crystallography https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 Aran, Martin Smal, Clara Pelliza, Leonardo Gallo, Mariana Otero, Lisandro Horacio Klinke, Sebastian Goldbaum, Fernando Alberto Ithurralde, Esteban Bercovich, Andrés Mac Cormack, Walter P. Turjanski, Adrian G. Cicero, Daniel Oscar Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain |
title | Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain |
title_full | Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain |
title_fullStr | Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain |
title_full_unstemmed | Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain |
title_short | Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain |
title_sort | solution and crystal structure of ba42, a protein from the antarctic bacterium bizionia argentinensis comprised of a stand-alone tpm domain |
topic | Structural Genomics Antarctic Bacteria Bizionia Argentinensis Ba42 Protein Structure Nuclear Magnetic Resonance X-Ray Crystallography https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
topic_facet | Structural Genomics Antarctic Bacteria Bizionia Argentinensis Ba42 Protein Structure Nuclear Magnetic Resonance X-Ray Crystallography https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
url | http://hdl.handle.net/11336/8535 |