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==Crystal structure of a mutant Staphylococcus equorum manganese superoxide dismutase S126C== | ==Crystal structure of a mutant Staphylococcus equorum manganese superoxide dismutase S126C== | ||
<StructureSection load='7ddw' size='340' side='right'caption='[[7ddw]]' scene=''> | <StructureSection load='7ddw' size='340' side='right'caption='[[7ddw]], [[Resolution|resolution]] 1.88Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DDW FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ddw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43958 Atcc 43958]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DDW FirstGlance]. <br> | ||
</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=7ddw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ddw OCA], [https://pdbe.org/7ddw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ddw RCSB], [https://www.ebi.ac.uk/pdbsum/7ddw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ddw ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5x2j|5x2j]], [[6m30|6m30]]</div></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AST02_02815 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246432 ATCC 43958])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Superoxide_dismutase Superoxide dismutase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=7ddw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ddw OCA], [https://pdbe.org/7ddw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ddw RCSB], [https://www.ebi.ac.uk/pdbsum/7ddw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ddw ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/A0A1E5TT85_9STAP A0A1E5TT85_9STAP]] 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 == | |||
The dimeric form of manganese superoxide dismutase is instrumental for activity because each of the monomers provides amino acid residues participating in the enzymatic reaction. Hence, preventing dissociation of the dimer would maintain the enzymatic activity in detrimental conditions e.g. high temperature. To prevent dissociation of the dimer, a disulphide (S-S) bond was introduced at the dimer interface. In the wild type structure, S126 interacts with S126 of the other monomer. In the presented work, a mutant was designed with an S126C substitution. The crystal structure of the S126C mutant showed that only 50-70% of monomers formed the S-S bond. This observed imperfect S-S bonding was likely caused by photolytic S-S bond breakage mediated by the neighbouring tryptophan residue. In the wild type, S126 is located facing W163 and forms a water-mediated hydrogen bond with E164; W163 and E164 are crucial in the enzyme's activity. The replacement of S126 by a cysteine residue lowered the activity of the enzyme by ~70%. S126 has never been considered to play a role in the enzyme's activity or stability, thus the finding showed the importance of this residue. | |||
The role of S126 in the Staphylococcus equorum MnSOD activity and stability.,Retnoningrum DS, Yoshida H, Razani MD, Muliadi R, Meidianto VF, Artarini A, Ismaya WT J Struct Biol. 2021 Mar 29;213(2):107731. doi: 10.1016/j.jsb.2021.107731. PMID:33794368<ref>PMID:33794368</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ddw" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 43958]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Artarini A]] | [[Category: Superoxide dismutase]] | ||
[[Category: Hartanto A]] | [[Category: Artarini, A]] | ||
[[Category: Ismaya | [[Category: Hartanto, A]] | ||
[[Category: Meidianto | [[Category: Ismaya, W T]] | ||
[[Category: Razani | [[Category: Meidianto, V F]] | ||
[[Category: Retnoningrum | [[Category: Razani, M D]] | ||
[[Category: Yoshida H]] | [[Category: Retnoningrum, D S]] | ||
[[Category: Yoshida, H]] | |||
[[Category: Disulfide bond]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Staphylococcus equorum]] | |||
Revision as of 10:02, 14 April 2021
Crystal structure of a mutant Staphylococcus equorum manganese superoxide dismutase S126CCrystal structure of a mutant Staphylococcus equorum manganese superoxide dismutase S126C
Structural highlights
Function[A0A1E5TT85_9STAP] Destroys radicals which are normally produced within the cells and which are toxic to biological systems.[RuleBase:RU000414] Publication Abstract from PubMedThe dimeric form of manganese superoxide dismutase is instrumental for activity because each of the monomers provides amino acid residues participating in the enzymatic reaction. Hence, preventing dissociation of the dimer would maintain the enzymatic activity in detrimental conditions e.g. high temperature. To prevent dissociation of the dimer, a disulphide (S-S) bond was introduced at the dimer interface. In the wild type structure, S126 interacts with S126 of the other monomer. In the presented work, a mutant was designed with an S126C substitution. The crystal structure of the S126C mutant showed that only 50-70% of monomers formed the S-S bond. This observed imperfect S-S bonding was likely caused by photolytic S-S bond breakage mediated by the neighbouring tryptophan residue. In the wild type, S126 is located facing W163 and forms a water-mediated hydrogen bond with E164; W163 and E164 are crucial in the enzyme's activity. The replacement of S126 by a cysteine residue lowered the activity of the enzyme by ~70%. S126 has never been considered to play a role in the enzyme's activity or stability, thus the finding showed the importance of this residue. The role of S126 in the Staphylococcus equorum MnSOD activity and stability.,Retnoningrum DS, Yoshida H, Razani MD, Muliadi R, Meidianto VF, Artarini A, Ismaya WT J Struct Biol. 2021 Mar 29;213(2):107731. doi: 10.1016/j.jsb.2021.107731. PMID:33794368[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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