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

• 영문명: Crystal structure of the N-terminal domain of Candida glabrata Hsp90
• 발행기관: 한국구조생물학회
• 저자명: Lingchen Tan Xiaojie Li Gongchun Zhang Lin Chen Young Jun Im
• 간행물 정보: 『Biodesign』Vol 12, No 2, Jun, 13~18쪽, 전체 6쪽
• 주제분류: 자연과학 > 생물학
• 파일형태: PDF
• 발행일자: 2024.06.30

국문 초록

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 replacement 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.

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INTRODUCTION

MATERIALS AND METHODS

RESULTS AND DISCUSSION

ACKNOWLEDGEMENTS

AUTHOR CONTRIBUTIONS

DATA AVAILABILITY

REFERENCES