View source for 8imd


==Crystal structure of Cu/Zn Superoxide dismutase from Paenibacillus lautus==
<StructureSection load='8imd' size='340' side='right'caption='[[8imd]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8imd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_lautus_NBRC_15380 Paenibacillus lautus NBRC 15380]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IMD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8imd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8imd OCA], [https://pdbe.org/8imd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8imd RCSB], [https://www.ebi.ac.uk/pdbsum/8imd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8imd ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cu/Zn-superoxide dismutase (CuZnSOD) is an enzyme that binds a copper and zinc ion and also forms an intramolecular disulfide bond. Together with the copper ion as the active site, the disulfide bond is completely conserved among these proteins; indeed, the disulfide bond plays critical roles in maintaining the catalytically competent conformation of CuZnSOD. Here, we found that a CuZnSOD protein in Paenibacillus lautus (PaSOD) has no Cys residue but exhibits a significant level of enzyme activity. The crystal structure of PaSOD revealed hydrophobic and hydrogen-bonding interactions in substitution for the disulfide bond of the other CuZnSOD proteins. Also notably, we determined that PaSOD forms a homodimer through an additional domain with a novel fold at the N terminus. While the advantages of lacking Cys residues and adopting a novel dimer configuration remain obscure, PaSOD does not require a disulfide-introducing/correcting system for maturation and could also avoid misfolding caused by aberrant thiol oxidations under an oxidative environment.

Characterization of a novel cysteine-less Cu/Zn-superoxide dismutase in Paenibacillus lautus missing a conserved disulfide bond.,Furukawa Y, Shintani A, Narikiyo S, Sue K, Akutsu M, Muraki N J Biol Chem. 2023 Aug;299(8):105040. doi: 10.1016/j.jbc.2023.105040. Epub 2023 , Jul 11. PMID:37442237<ref>PMID:37442237</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8imd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Paenibacillus lautus NBRC 15380]]
[[Category: Akutsu M]]
[[Category: Furukawa Y]]
[[Category: Narikiyo S]]