Loss of quaternary structure is associated with rapid sequence divergence in the OSBS family

The rate of protein evolution is determined by a combination of selective pressure on protein function and biophysical constraints on protein folding and structure. Determining the relative contributions of these properties is an unsolved problem in molecular evolution with broad implications for pr...

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Veröffentlicht in:Proceedings of the National Academy of Sciences - PNAS 2014-06, Vol.111 (23), p.8535-8540
Hauptverfasser: Odokonyero, Denis, Sakai, Ayano, Patskovsky, Yury, Malashkevich, Vladimir N., Fedorov, Alexander A., Bonanno, Jeffrey B., Fedorov, Elena V., Toro, Rafael, Agarwal, Rakhi, Wang, Chenxi, Ozerova, Nicole D. S., Yew, Wen Shan, Sauder, J. Michael, Swaminathan, Subramanyam, Burley, Stephen K., Almo, Steven C., Glasner, Margaret E.
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Sprache:eng
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Zusammenfassung:The rate of protein evolution is determined by a combination of selective pressure on protein function and biophysical constraints on protein folding and structure. Determining the relative contributions of these properties is an unsolved problem in molecular evolution with broad implications for protein engineering and function prediction. As a case study, we examined the structural divergence of the rapidly evolving o -succinylbenzoate synthase (OSBS) family, which catalyzes a step in menaquinone synthesis in diverse microorganisms and plants. On average, the OSBS family is much more divergent than other protein families from the same set of species, with the most divergent family members sharing
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1318703111