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The coupling between disulphide status, metallation and dimer interface strength in Cu/Zn superoxide dismutase.

Hörnberg A, Logan DT, Marklund SL, Oliveberg M
J Mol Biol 365 333-42 (2007)
Related entries: 2gbu, 2gbv

Cited: 61 times
EuropePMC logo PMID: 17070542

Abstract

The gain of neurotoxic function in amyotrophic lateral sclerosis (ALS) has been linked to misfolding of the homodimeric enzyme Cu/Zn superoxide dismutase (SOD). Here, we present the crystal structure of fully cysteine-depleted human SOD (SOD(CallA)), representing a reduced, marginally stable intermediate on the folding pathway in vivo that has also been implicated as neurotoxic precursor state. A hallmark of this species is that it fails to dimerize and becomes trapped as a monomer in the absence of the active-site metals. The crystallographic data show that removal of the C57-C146 disulphide bond sets free the interface loop IV in the apo protein, whereas the same loop remains unaffected in the holo protein. Thus, the low dimerisation propensity of disulphide-reduced apoSOD seems to be of entropic origin due to increased loop flexibility in the monomeric state: in the disulphide-reduced holo protein this gain in configurational entropy upon splitting of the dimer interface is reduced by the metal coordination.

Reviews - 2gbt mentioned but not cited (1)

  1. Structural Properties and Interaction Partners of Familial ALS-Associated SOD1 Mutants. Huai J, Zhang Z. Front Neurol 10 527 (2019)

Articles - 2gbt mentioned but not cited (1)

  1. Diffuse binding of Zn(2+) to the denatured ensemble of Cu/Zn superoxide dismutase 1. Szpryngiel S, Oliveberg M, Mäler L. FEBS Open Bio 5 56-63 (2015)


Reviews citing this publication (10)

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Articles citing this publication (49)

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  45. Native Mass Spectrometry Coupled to Spectroscopic Methods to Investigate the Effect of Soybean Isoflavones on Structural Stability and Aggregation of Zinc Deficient and Metal-Free Superoxide Dismutase. Bian X, Zhuang X, Xing J, Liu S, Liu Z, Song F. Molecules 27 7303 (2022)
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