Equilibrium folding intermediates of a Greek key beta-barrel protein

Journal of Molecular Biology
S BagbyA Chakrabartty

Abstract

Protein S is a calcium-binding protein comprising two Greek key beta-barrel domains. We have used NMR and optical spectroscopies to show that, in the absence of calcium, the N-terminal domain of protein S forms two equilibrium folding intermediates that are in slow exchange. The intermediates arise from differential calcium-dependent folding of subdomains which are not contiguous along the polypeptide chain. The structures of these intermediates are incompatible with several previously proposed folding mechanisms for Greek key beta-barrel domains. We proposed a different mechanism that involves multiple nucleation sites for folding and sequential acquisition of native long-range interactions.

Citations

Mar 13, 2001·Environmental Microbiology·H K HøidalS Valla
Aug 5, 1998·Proceedings of the National Academy of Sciences of the United States of America·M CompianiR Casadio
Mar 25, 2011·Protein Science : a Publication of the Protein Society·Fanrong Kong, Jonathan King
Oct 2, 2007·Protein Science : a Publication of the Protein Society·Ishara A MillsJonathan A King
Nov 14, 2001·The Journal of Biological Chemistry·Andrew G PurkissChristine Slingsby
Sep 5, 2001·European Journal of Biochemistry·X F QiA Chakrabartty
Aug 8, 2006·The Journal of Biological Chemistry·Shannon L FlaughJonathan King
Mar 5, 2019·Advanced Science·Jaehun LeeKi Tae Nam
May 9, 2013·International Journal of Cosmetic Science·A RibeiroA M Cavaco-Paulo
Oct 19, 2005·Biochemistry·Alka Prasad, Susan Pedigo

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