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Control activity of yeast geranylgeranyl diphosphate synthase from dimer interface through H-bonds and hydrophobic interaction.

Biochemistry - 23 Apr 2013

Chang Chih-Kang, Teng Kuo-Hsun, Lin Sheng-Wei, Chang Tao-Hsin, Liang Po-Huang

Abstract excerpt

Previously we showed that yeast geranylgeranyl diphosphate synthase (GGPPS) becomes an inactive monomer when the first N-terminal helix involved in dimerization is deleted. This raises questions regarding why dimerization is required for GGPPS activity and which amino acids in the dimer interface are essential for dimerization-mediated activity. According to the GGPPS crystal structure, three amino acids (N101,...

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PMID: 23534508
DOI: 10.1021/bi4001276

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