MS09-P04 Crystal structure of inositol 1,3,4,5,6-pentakisphosphate 2-kinase from Cryptococcus neoformans Sangkee Rhee (Department of Agricultural Biotechnology, Seoul National University, SEOUL, Korea South) Juntaek Oh (Department of Agricultural Biotechnology, Seoul National University, SEOUL, Korea South) Dong-Gi Lee (Department of Biotechnology, Yonsei University, SEOUL, Korea South) Yong-Sun Bahn (Department of Biotechnology, Yonsei University, SEOUL, Korea South)email: srheesnu@snu.ac.krThe fungal pathogen Cryptococcus neoformans is a causative agent of meningoencephalitis in humans. For its pathogenicity, the inositol polyphosphate biosynthetic pathway plays critical roles. In particular, an inositol 1,3,4,5,6-pentakisphosphate 2-kinase (Ipk1) catalyzes the phosphorylation of IP5 to form IP6, a substrate for subsequent reaction to produce inositol pyrophosphates, such as PP-IP5/IP7. In fact, deletion of IPK1 significantly reduces the virulence of C. neoformans, indicating that Ipk1 from C. neoformans (CnIpk1) is a major virulence contributor. We initiated structural analysis of CnIpk1 to provide structural information for the possible development of drug design for treatment of cryptococcosis. A crystal structure of the unliganded CnIpk1, the first structure for a fungal Ipk1, will be presented at 2.35 Å resolution. Structure comparisons of CnIpk1 with those from Arabidopsis thaliana and Mus musculus suggest structural similarities and discrepancies for fungal Ipk1 among members of the Ipk1 family. This work was supported by Next Generation BioGreen 21 program of Rural Development Administration (Plant Molecular Breeding Center) of Republic of KOREA.References:

Oh, J. Lee, D.-G. Bahn, Y.-S. & Rhee, S. (2017) J. Struct. Biol. 200, 118-123.
Keywords: inositol 1,3,4,5,6-pentakisphosphate 2-kinase; Cryptococcus neoformans; crystal structure