4XCR

Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form, mutant I35A

Summary for 4XCR

• Entry DOI: 10.2210/pdb4xcr/pdb
• Descriptor: Superoxide dismutase [Cu-Zn] (1 entity in total)
• Functional Keywords: oxidoreductase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 21896.42

Authors

Wang, H.,Logan, D.T.,Danielsson, J.,Mu, X.,Binolfi, A.,Theillet, F.,Bekei, B.,Lang, L.,Wennerstrom, H.,Selenko, P.,Oliveberg, M. (deposition date: 2014-12-18, release date: 2016-01-20, Last modification date: 2024-01-10)

Primary citation

Danielsson, J.,Mu, X.,Lang, L.,Wang, H.,Binolfi, A.,Theillet, F.X.,Bekei, B.,Logan, D.T.,Selenko, P.,Wennerstrom, H.,Oliveberg, M.
Thermodynamics of protein destabilization in live cells.
Proc. Natl. Acad. Sci. U.S.A., 112:12402-12407, 2015

PubMed Abstract: Although protein folding and stability have been well explored under simplified conditions in vitro, it is yet unclear how these basic self-organization events are modulated by the crowded interior of live cells. To find out, we use here in-cell NMR to follow at atomic resolution the thermal unfolding of a β-barrel protein inside mammalian and bacterial cells. Challenging the view from in vitro crowding effects, we find that the cells destabilize the protein at 37 °C but with a conspicuous twist: While the melting temperature goes down the cold unfolding moves into the physiological regime, coupled to an augmented heat-capacity change. The effect seems induced by transient, sequence-specific, interactions with the cellular components, acting preferentially on the unfolded ensemble. This points to a model where the in vivo influence on protein behavior is case specific, determined by the individual protein's interplay with the functionally optimized "interaction landscape" of the cellular interior.

PubMed: 26392565
DOI: 10.1073/pnas.1511308112

Experimental method

X-RAY DIFFRACTION (3.602 Å)