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6ELK

C.elegans MnSOD-3 mutant - Q142H

Summary for 6ELK
Entry DOI10.2210/pdb6elk/pdb
Related3DC5 4X9Q
DescriptorSuperoxide dismutase [Mn] 2, mitochondrial, MANGANESE (II) ION, SULFATE ION, ... (5 entities in total)
Functional Keywordssuperoxide dismutase, manganese, oxidoreductase
Biological sourceCaenorhabditis elegans
Cellular locationMitochondrion : P41977
Total number of polymer chains2
Total formula weight45517.34
Authors
Hunter, G.J.,Trinh, C.H.,Hunter, T. (deposition date: 2017-09-29, release date: 2017-12-06, Last modification date: 2024-01-17)
Primary citationHunter, T.,Bonetta, R.,Sacco, A.,Vella, M.,Sultana, P.M.,Trinh, C.H.,Fadia, H.B.R.,Borowski, T.,Garcia-Fandino, R.,Stockner, T.,Hunter, G.J.
A Single Mutation is Sufficient to Modify the Metal Selectivity and Specificity of a Eukaryotic Manganese Superoxide Dismutase to Encompass Iron.
Chemistry, 24:5303-5308, 2018
Cited by
PubMed Abstract: We have generated a site-directed mutant of the manganese superoxide dismutase SOD-3 of C.elegans (MnSOD-3) which modifies the metal specificity of the enzyme. While wild-type MnSOD-3 functions with manganese in the active site (3600 U mg of protein) it has little or no activity when iron is incorporated. However, when histidine replaces glutamine 142 in the active site, the enzyme retains 50 % of its activity and becomes cambialistic for its metal cofactor exhibiting very similar specific activity with either manganese or iron.
PubMed: 29178484
DOI: 10.1002/chem.201704655
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

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