1s4i

<StructureSection load='1s4i' size='340' side='right' caption='[[1s4i]], [[Resolution|resolution]] 1.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[1s4i]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S4I FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YOJM, BSU19400 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1s4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s4i OCA], [http://pdbe.org/1s4i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s4i RCSB], [http://www.ebi.ac.uk/pdbsum/1s4i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s4i ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:15897454</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1s4i" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Vibrio subtilis ehrenberg 1835]]

[[Category: Superoxide dismutase]]

[[Category: Banci, L]]

[[Category: Bertini, I]]

[[Category: Calderone, V]]

[[Category: Conte, R Del]]

[[Category: Cramaro, F]]

[[Category: Fantoni, A]]

[[Category: Mangani, S]]

[[Category: Quattrone, A]]

[[Category: Viezzoli, M S]]

[[Category: Sod-like]]