| Structural highlights
Disease
[SODC_HUMAN] Defects in SOD1 are the cause of amyotrophic lateral sclerosis type 1 (ALS1) [MIM:105400]. ALS1 is a familial form of amyotrophic lateral sclerosis, a neurodegenerative disorder affecting upper and lower motor neurons and resulting in fatal paralysis. Sensory abnormalities are absent. Death usually occurs within 2 to 5 years. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of cases leading to familial forms.[1] [2] [3] [4] [5] [6] [7] [8] [:][9] [10] [11] [12] [13] [14] [15] [16] [17] [18] [19] [20] [21] [22] [23] [24] [25] [26] [27] [28] [29] [30] [31] [32] [33] [34] [35] [36] [37] [38] [39] [40] [41] [42] [43] [44] [45]
Function
[SODC_HUMAN] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. [CCS1_YEAST] Copper chaperone for apo superoxide dismutase 1 (SOD1). Binds copper ions and delivers them specifically to apo-SOD1.[46]
Publication Abstract from PubMed
Metallochaperones are a diverse family of trafficking molecules that provide metal ions to protein targets for use as cofactors. The copper chaperone for superoxide dismutase (Ccs1) activates immature copper-zinc superoxide dismutase (Sod1) by delivering copper and facilitating the oxidation of the Sod1 intramolecular disulfide bond. Here, we present structural, spectroscopic, and cell-based data supporting a novel copper-induced mechanism for Sod1 activation. Ccs1 binding exposes an electropositive cavity and proposed "entry site" for copper ion delivery on immature Sod1. Copper-mediated sulfenylation leads to a sulfenic acid intermediate that eventually resolves to form the Sod1 disulfide bond with concomitant release of copper into the Sod1 active site. Sod1 is the predominant disulfide bond-requiring enzyme in the cytoplasm, and this copper-induced mechanism of disulfide bond formation obviates the need for a thiol/disulfide oxidoreductase in that compartment.
Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site.,Fetherolf MM, Boyd SD, Taylor AB, Kim HJ, Wohlschlegel JA, Blackburn NJ, Hart PJ, Winge DR, Winkler DD J Biol Chem. 2017 Jul 21;292(29):12025-12040. doi: 10.1074/jbc.M117.775981. Epub , 2017 May 22. PMID:28533431[47]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
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- ↑ Fetherolf MM, Boyd SD, Taylor AB, Kim HJ, Wohlschlegel JA, Blackburn NJ, Hart PJ, Winge DR, Winkler DD. Copper-zinc superoxide dismutase is activated through a sulfenic acid intermediate at a copper ion entry site. J Biol Chem. 2017 Jul 21;292(29):12025-12040. doi: 10.1074/jbc.M117.775981. Epub , 2017 May 22. PMID:28533431 doi:http://dx.doi.org/10.1074/jbc.M117.775981
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