Characterization of monomeric dihydrodipicolinate synthase variant reveals the importance of substrate binding in optimizing oligomerization

Article ID	Journal	Published Year	Pages	File Type
7561348	Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics	2011	10 Pages	PDF

Abstract

âº Examined the role of electrostatic charges at protein interfaces. âº Removal of charged residues destabilized quaternary structure. âº Removal of charged residues reduced heat stability. âº Binding of substrate impacts quaternary structure and stability.

Keywords

RMSD NAL Dihydrodipicolinate reductase DHDPS Dihydrodipicolinate synthase root-mean-square deviation Thermotoga maritima Quaternary structure Cooperative assembly HtpA Thermal stability

Related Topics

Physical Sciences and Engineering Chemistry Analytical Chemistry

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Characterization of monomeric dihydrodipicolinate synthase variant reveals the importance of substrate binding in optimizing oligomerization

Authors

F. Grant Pearce, Renwick C.J. Dobson, Geoffrey B. Jameson, Matthew A. Perugini, Juliet A. Gerrard,