Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder.

ABSTRACT: Protein-engineering methods (Phi-values) were used to investigate the folding transition state of a lysin motif (LysM) domain from Escherichia coli membrane-bound lytic murein transglycosylase D. This domain consists of just 48 structured residues in a symmetrical betaalphaalphabeta arrangement and is the smallest alphabeta protein yet investigated using these methods. An extensive mutational analysis revealed a highly robust folding pathway with no detectable transition state plasticity, indicating that LysM is an example of an ideal two-state folder. The pattern of Phi-values denotes a highly polarised transition state, with significant formation of the helices but no structure within the beta-sheet. Remarkably, this transition state remains polarised after circularisation of the domain,

SUBMITTER: Nickson AA 

PROVIDER: S-EPMC2441773 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature