pISSN 2288-6982
eISSN 2288-7105




BioDesign 2024; 12(2): 13-18

Published online June 30, 2024

© Korean Society for Structural Biology

Crystal structure of the N-terminal domain of Candida glabrata Hsp90

Lingchen Tan, Xiaojie Li, Gongchun Zhang, Lin Chen and Young Jun Im*

College of Pharmacy, Chonnam National University, Gwangju 61186, Republic of Korea

Correspondence to:

Received: April 11, 2024; Revised: May 1, 2024; Accepted: June 4, 2024


Hsp90 is a molecular chaperone that promotes protein folding and maturation of various client proteins. In this study, we purified Candida glabrata Hsp90 and crystallized the protein in 100 mM HEPES-NaOH pH7.5, 70% 2-methyl-2,4- pentanediol. We collected the x-ray diffraction data to 1.9 Å resolution. The crystals belong to the space group P4322 with unit cell parameters a = b = 73.9 Å, and c = 108.7 Å. Solvent content analysis suggested that a proteolytic fragment of the full-length formed the crystals. We determined the structure of the ATP-binding N-terminal domain (NTD) by molecular replacient using a structure of S. cerevisiae Hsc82. The asymmetric unit contained one NTD with a solvent content of 59.5%. The structure of CgHsp90 NTD spanning the residues 2-212 was refined to the Rfree factor of 22.7%. The structure reveals an open conformation of the nucleotide-binding site and structural conservation of the NTDs in fungal Hsp90 proteins.