1u3n
From Proteopedia
(New page: 200px<br /><applet load="1u3n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u3n" /> '''A SOD-like protein from B. subtilis, unstruc...) |
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| - | [[Image:1u3n.gif|left|200px]]<br /><applet load="1u3n" size=" | + | [[Image:1u3n.gif|left|200px]]<br /><applet load="1u3n" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1u3n" /> | caption="1u3n" /> | ||
'''A SOD-like protein from B. subtilis, unstructured in solution, becomes ordered in the crystal: implications for function and for fibrillogenesis'''<br /> | '''A SOD-like protein from B. subtilis, unstructured in solution, becomes ordered in the crystal: implications for function and for fibrillogenesis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Little is known about prokaryotic homologs of Cu,Zn superoxide dismutase | + | 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 beta-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. |
==About this Structure== | ==About this Structure== | ||
| - | 1U3N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http:// | + | 1U3N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U3N OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bertini, I.]] | [[Category: Bertini, I.]] | ||
[[Category: Calderone, V.]] | [[Category: Calderone, V.]] | ||
| - | [[Category: Conte, R | + | [[Category: Conte, R Del.]] |
[[Category: Cramaro, F.]] | [[Category: Cramaro, F.]] | ||
[[Category: Fantoni, A.]] | [[Category: Fantoni, A.]] | ||
[[Category: Mangani, S.]] | [[Category: Mangani, S.]] | ||
[[Category: Quattrone, A.]] | [[Category: Quattrone, A.]] | ||
| - | [[Category: Viezzoli, M | + | [[Category: Viezzoli, M S.]] |
[[Category: sod-like; bacillus subtilis; bssod; solution structure; nmr; metalloprotein]] | [[Category: sod-like; bacillus subtilis; bssod; solution structure; nmr; metalloprotein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:18 2008'' |
Revision as of 13:20, 21 February 2008
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A SOD-like protein from B. subtilis, unstructured in solution, becomes ordered in the crystal: implications for function and for fibrillogenesis
Overview
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 beta-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.
About this Structure
1U3N is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystal., Banci L, Bertini I, Calderone V, Cramaro F, Del Conte R, Fantoni A, Mangani S, Quattrone A, Viezzoli MS, Proc Natl Acad Sci U S A. 2005 May 24;102(21):7541-6. Epub 2005 May 16. PMID:15897454
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