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...
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todo:paper_08873585_v82_n11_p3062_Aran2023-10-03T15:40:53Z Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain Aran, M. Smal, C. Pellizza, L. Gallo, M. Otero, L.H. Klinke, S. Goldbaum, F.A. Ithurralde, E.R. Bercovich, A. Mac Cormack, W.P. Turjanski, A.G. Cicero, D.O. Antarctic bacteria BA42 Bizionia argentinensis Nuclear magnetic resonance Protein structure Structural genomics X-ray crystallography ba42 protein bacterial protein metal ion unclassified drug bacterial protein calcium metal Article beta sheet binding affinity binding site Bizionia argentinensis crystal structure Flavobacterium metal binding molecular dynamics nonhuman nuclear magnetic resonance priority journal protein domain protein family protein stability X ray crystallography amino acid sequence animal Antarctica chemical structure chemistry circular dichroism Flavobacteriaceae genetics metabolism molecular genetics protein conformation protein tertiary structure sequence homology Bacteria (microorganisms) Bizionia Flavobacterium Amino Acid Sequence Animals Antarctic Regions Bacterial Proteins Binding Sites Calcium Circular Dichroism Crystallography, X-Ray Flavobacteriaceae Metals Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Stability Protein Structure, Tertiary Sequence Homology, Amino Acid 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. © 2014 Wiley Periodicals, Inc. Fil:Aran, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Smal, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Gallo, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Klinke, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Mac Cormack, W.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Turjanski, A.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Cicero, D.O. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_08873585_v82_n11_p3062_Aran |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Antarctic bacteria BA42 Bizionia argentinensis Nuclear magnetic resonance Protein structure Structural genomics X-ray crystallography ba42 protein bacterial protein metal ion unclassified drug bacterial protein calcium metal Article beta sheet binding affinity binding site Bizionia argentinensis crystal structure Flavobacterium metal binding molecular dynamics nonhuman nuclear magnetic resonance priority journal protein domain protein family protein stability X ray crystallography amino acid sequence animal Antarctica chemical structure chemistry circular dichroism Flavobacteriaceae genetics metabolism molecular genetics protein conformation protein tertiary structure sequence homology Bacteria (microorganisms) Bizionia Flavobacterium Amino Acid Sequence Animals Antarctic Regions Bacterial Proteins Binding Sites Calcium Circular Dichroism Crystallography, X-Ray Flavobacteriaceae Metals Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Stability Protein Structure, Tertiary Sequence Homology, Amino Acid |
| spellingShingle |
Antarctic bacteria BA42 Bizionia argentinensis Nuclear magnetic resonance Protein structure Structural genomics X-ray crystallography ba42 protein bacterial protein metal ion unclassified drug bacterial protein calcium metal Article beta sheet binding affinity binding site Bizionia argentinensis crystal structure Flavobacterium metal binding molecular dynamics nonhuman nuclear magnetic resonance priority journal protein domain protein family protein stability X ray crystallography amino acid sequence animal Antarctica chemical structure chemistry circular dichroism Flavobacteriaceae genetics metabolism molecular genetics protein conformation protein tertiary structure sequence homology Bacteria (microorganisms) Bizionia Flavobacterium Amino Acid Sequence Animals Antarctic Regions Bacterial Proteins Binding Sites Calcium Circular Dichroism Crystallography, X-Ray Flavobacteriaceae Metals Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Stability Protein Structure, Tertiary Sequence Homology, Amino Acid Aran, M. Smal, C. Pellizza, L. Gallo, M. Otero, L.H. Klinke, S. Goldbaum, F.A. Ithurralde, E.R. Bercovich, A. Mac Cormack, W.P. Turjanski, A.G. Cicero, D.O. Solution and crystal structure of BA42, a protein from the Antarctic bacterium Bizionia argentinensis comprised of a stand-alone TPM domain |
| topic_facet |
Antarctic bacteria BA42 Bizionia argentinensis Nuclear magnetic resonance Protein structure Structural genomics X-ray crystallography ba42 protein bacterial protein metal ion unclassified drug bacterial protein calcium metal Article beta sheet binding affinity binding site Bizionia argentinensis crystal structure Flavobacterium metal binding molecular dynamics nonhuman nuclear magnetic resonance priority journal protein domain protein family protein stability X ray crystallography amino acid sequence animal Antarctica chemical structure chemistry circular dichroism Flavobacteriaceae genetics metabolism molecular genetics protein conformation protein tertiary structure sequence homology Bacteria (microorganisms) Bizionia Flavobacterium Amino Acid Sequence Animals Antarctic Regions Bacterial Proteins Binding Sites Calcium Circular Dichroism Crystallography, X-Ray Flavobacteriaceae Metals Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Stability Protein Structure, Tertiary Sequence Homology, Amino Acid |
| 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. © 2014 Wiley Periodicals, Inc. |
| format |
JOUR |
| author |
Aran, M. Smal, C. Pellizza, L. Gallo, M. Otero, L.H. Klinke, S. Goldbaum, F.A. Ithurralde, E.R. Bercovich, A. Mac Cormack, W.P. Turjanski, A.G. Cicero, D.O. |
| author_facet |
Aran, M. Smal, C. Pellizza, L. Gallo, M. Otero, L.H. Klinke, S. Goldbaum, F.A. Ithurralde, E.R. Bercovich, A. Mac Cormack, W.P. Turjanski, A.G. Cicero, D.O. |
| author_sort |
Aran, M. |
| title |
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_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_sort |
solution and crystal structure of ba42, a protein from the antarctic bacterium bizionia argentinensis comprised of a stand-alone tpm domain |
| url |
http://hdl.handle.net/20.500.12110/paper_08873585_v82_n11_p3062_Aran |
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