1s4i
From Proteopedia
(New page: 200px<br /><applet load="1s4i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s4i, resolution 1.80Å" /> '''Crystal structure of...) |
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| - | [[Image:1s4i.gif|left|200px]]<br /><applet load="1s4i" size=" | + | [[Image:1s4i.gif|left|200px]]<br /><applet load="1s4i" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1s4i, resolution 1.80Å" /> | caption="1s4i, resolution 1.80Å" /> | ||
'''Crystal structure of a SOD-like protein from Bacillus subtilis'''<br /> | '''Crystal structure of a SOD-like protein from Bacillus subtilis'''<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== | ||
| - | 1S4I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ZN and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Full crystallographic information is available from [http:// | + | 1S4I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4I 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: CL]] | [[Category: CL]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: superoxide dismutase]] | [[Category: superoxide dismutase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:57:56 2008'' |
Revision as of 12:57, 21 February 2008
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Crystal structure of a SOD-like protein from Bacillus subtilis
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
1S4I is a Single protein structure of sequence from Bacillus subtilis with and as ligands. Active as Superoxide dismutase, with EC number 1.15.1.1 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
Page seeded by OCA on Thu Feb 21 14:57:56 2008
Categories: Bacillus subtilis | Single protein | Superoxide dismutase | Banci, L. | Bertini, I. | Calderone, V. | Conte, R Del. | Cramaro, F. | Fantoni, A. | Mangani, S. | Quattrone, A. | Viezzoli, M S. | CL | ZN | Cu-zn sod | Sod | Sod-like
