View source for 7sbh


==Crystal structure of the iron superoxide dismutase from Acinetobacter sp. Ver3==
<StructureSection load='7sbh' size='340' side='right'caption='[[7sbh]], [[Resolution|resolution]] 1.34&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7sbh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_sp._Ver3 Acinetobacter sp. Ver3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SBH 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]] 1.34&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=7sbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sbh OCA], [https://pdbe.org/7sbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sbh RCSB], [https://www.ebi.ac.uk/pdbsum/7sbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sbh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A031LR83_9GAMM A0A031LR83_9GAMM] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Acinetobacter sp. Ver3 is a polyextremophilic strain characterized by a high tolerance to radiation and pro-oxidants. The Ver3 genome comprises the sodB and sodC genes encoding an iron ((AV3)SodB) and a copper/zinc superoxide dismutase ((AV3)SodC), respectively; however, the specific role(s) of these genes has remained elusive. We show that the expression of sodB remained unaltered in different oxidative stress conditions whereas sodC was up-regulated in the presence of blue light. Besides, we studied the changes in the in vitro activity of each SOD enzyme in response to diverse agents and solved the crystal structure of (AV3)SodB at 1.34 A, one of the highest resolutions achieved for a SOD. Cell fractionation studies interestingly revealed that (AV3)SodB is located in the cytosol whereas (AV3)SodC is also found in the periplasm. Consistently, a bioinformatic analysis of the genomes of 53 Acinetobacter species pointed out the presence of at least one SOD type in each compartment, suggesting that these enzymes are separately required to cope with oxidative stress. Surprisingly, (AV3)SodC was found in an active state also in outer membrane vesicles, probably exerting a protective role. Overall, our multidisciplinary approach highlights the relevance of SOD enzymes when Acinetobacter spp. are confronted with oxidizing agents.

The distinctive roles played by the superoxide dismutases of the extremophile Acinetobacter sp. Ver3.,Steimbruch BA, Sartorio MG, Cortez N, Albanesi D, Lisa MN, Repizo GD Sci Rep. 2022 Mar 12;12(1):4321. doi: 10.1038/s41598-022-08052-z. PMID:35279679<ref>PMID:35279679</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7sbh" style="background-color:#fffaf0;"></div>

==See Also==
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acinetobacter sp. Ver3]]
[[Category: Large Structures]]
[[Category: Albanesi D]]
[[Category: Lisa MN]]
[[Category: Repizo GD]]
[[Category: Steimbruch BA]]