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A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal.

Little is known about prokaryotic homologs of Cu,Zn superoxide dismutase (SOD), an enzyme highly conserved among eukaryotic species. In 138 Archaea and Bacteria genomes, 57 of these putative homologs were found, 11 of which lack at least one of the metal ligands. Both the solution and the crystal st... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America May 24, 2005, Vol.102(21), pp.7541-7546
Main Author: Banci, Lucia
Other Authors: Bertini, Ivano , Calderone, Vito , Cramaro, Fiorenza , Del Conte, Rebecca , Fantoni, Adele , Mangani, Stefano , Quattrone, Alessandro , Viezzoli, Maria Silvia
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0027-8424
Link: http://search.proquest.com/docview/67864349/?pq-origsite=primo
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title: A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal.
format: Article
creator:
  • Banci, Lucia
  • Bertini, Ivano
  • Calderone, Vito
  • Cramaro, Fiorenza
  • Del Conte, Rebecca
  • Fantoni, Adele
  • Mangani, Stefano
  • Quattrone, Alessandro
  • Viezzoli, Maria Silvia
subjects:
  • Amino Acid Sequence–Genetics
  • Bacillus Subtilis–Metabolism
  • Computational Biology–Genetics
  • Crystallography, X-Ray–Metabolism
  • Dimerization–Ultrastructure
  • Genome, Archaeal–Ultrastructure
  • Genome, Bacterial–Ultrastructure
  • Genomics–Ultrastructure
  • Ligands–Ultrastructure
  • Magnetic Resonance Spectroscopy–Ultrastructure
  • Models, Molecular–Ultrastructure
  • Molecular Sequence Data–Ultrastructure
  • Phylogeny–Ultrastructure
  • Protein Structure, Tertiary–Ultrastructure
  • Sequence Alignment–Ultrastructure
  • Superoxide Dismutase–Ultrastructure
  • Ligands
  • Superoxide Dismutase
ispartof: Proceedings of the National Academy of Sciences of the United States of America, May 24, 2005, Vol.102(21), pp.7541-7546
description: Little is known about prokaryotic homologs of Cu,Zn superoxide dismutase (SOD), an enzyme highly conserved among eukaryotic species. In 138 Archaea and Bacteria genomes, 57 of these putative homologs were found, 11 of which lack at least one of the metal ligands. Both the solution and the crystal structures of the SOD-like protein from Bacillus subtilis, lacking two Cu ligands and found to be enzymatically inactive, were determined. In solution, the protein is monomeric. The available nuclear Overhauser effects, together with chemical-shift index values, allowed us to define and to recognize the typical Cu,Zn SOD Greek E-barrel but with largely unstructured loops (which, therefore, sample a wide range of conformations). On the contrary, in the crystal structure (obtained in the presence of slight excess of Zn), the protein is well structured and organized in covalent dimers held by a symmetric bridge consisting of a Zn ion bound to an Asp-His dyad in a tetrahedral geometry. Couples of dimers held by hydrophobic interactions and H bonds are further organized in long chains. The order/disorder transition is discussed in terms of metal binding and physical state. conformational mobility | NMR structure determination | Zn-mediated protein dimers | x-ray crystallography | superoxide dismutase
language: eng
source:
identifier: ISSN: 0027-8424
fulltext: fulltext
issn:
  • 00278424
  • 0027-8424
url: Link


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titleA prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal.
creatorBanci, Lucia ; Bertini, Ivano ; Calderone, Vito ; Cramaro, Fiorenza ; Del Conte, Rebecca ; Fantoni, Adele ; Mangani, Stefano ; Quattrone, Alessandro ; Viezzoli, Maria Silvia
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ispartofProceedings of the National Academy of Sciences of the United States of America, May 24, 2005, Vol.102(21), pp.7541-7546
identifierISSN: 0027-8424
subjectAmino Acid Sequence–Genetics ; Bacillus Subtilis–Metabolism ; Computational Biology–Genetics ; Crystallography, X-Ray–Metabolism ; Dimerization–Ultrastructure ; Genome, Archaeal–Ultrastructure ; Genome, Bacterial–Ultrastructure ; Genomics–Ultrastructure ; Ligands–Ultrastructure ; Magnetic Resonance Spectroscopy–Ultrastructure ; Models, Molecular–Ultrastructure ; Molecular Sequence Data–Ultrastructure ; Phylogeny–Ultrastructure ; Protein Structure, Tertiary–Ultrastructure ; Sequence Alignment–Ultrastructure ; Superoxide Dismutase–Ultrastructure ; Ligands ; Superoxide Dismutase
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descriptionLittle is known about prokaryotic homologs of Cu,Zn superoxide dismutase (SOD), an enzyme highly conserved among eukaryotic species. In 138 Archaea and Bacteria genomes, 57 of these putative homologs were found, 11 of which lack at least one of the metal ligands. Both the solution and the crystal structures of the SOD-like protein from Bacillus subtilis, lacking two Cu ligands and found to be enzymatically inactive, were determined. In solution, the protein is monomeric. The available nuclear Overhauser effects, together with chemical-shift index values, allowed us to define and to recognize the typical Cu,Zn SOD Greek E-barrel but with largely unstructured loops (which, therefore, sample a wide range of conformations). On the contrary, in the crystal structure (obtained in the presence of slight excess of Zn), the protein is well structured and organized in covalent dimers held by a symmetric bridge consisting of a Zn ion bound to an Asp-His dyad in a tetrahedral geometry. Couples of dimers held by hydrophobic interactions and H bonds are further organized in long chains. The order/disorder transition is discussed in terms of metal binding and physical state. conformational mobility | NMR structure determination | Zn-mediated protein dimers | x-ray crystallography | superoxide dismutase
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titleA prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal.
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titleA prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal.
authorBanci, Lucia ; Bertini, Ivano ; Calderone, Vito ; Cramaro, Fiorenza ; Del Conte, Rebecca ; Fantoni, Adele ; Mangani, Stefano ; Quattrone, Alessandro ; Viezzoli, Maria Silvia
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atitleA prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal.
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