7VF4

Crystal structure of Vps75 from Candida albicans

Summary for 7VF4

• Entry DOI: 10.2210/pdb7vf4/pdb
• Descriptor: Vps75, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: candida albicans, vps75, histone chaperon, histone lysine acetylation, rtt109, chaperone
• Biological source: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
• Total number of polymer chains: 8
• Total formula weight: 224701.28

Authors

Wang, W.,Chen, X.,Yang, Z.,Chen, X.,Li, C.,Wang, M. (deposition date: 2021-09-10, release date: 2021-10-06, Last modification date: 2023-11-29)

Primary citation

Wang, W.,Chen, X.,Yang, Z.,Chen, X.,Li, C.,Wang, M.
Crystal structure of histone chaperone Vps75 from Candida albicans.
Biochem.Biophys.Res.Commun., 578:136-141, 2021

PubMed Abstract: Vps75 is a histone chaperone that interacts with the fungal-specific histone acetyltransferase Rtt109 and stimulates its acetylation activity on histone H3. Here we report the crystal structure of Vps75 of Candida albicans, one of the most common fungal pathogens. CaVps75 exists as a headphone-like dimer that forms a large negatively charged region on its concave side, showing the potential to bind positively charged regions of histones. The distal ends of the concave side of the CaVps75 dimer are positively charged and each has one more α helix than yeast Vps75. CaVps75 exhibits ionic strength- and concentration-dependent higher oligomerization in solution. In the crystal, two dimers are bound through electrostatic interactions between charged regions on the concave side of their earmuff domains, and this inter-dimer interaction differs from the currently known inter-dimer interactions of Vps75s. Our results will help to understand the role of Vps75 in C. albicans.

PubMed: 34562653
DOI: 10.1016/j.bbrc.2021.09.030

Experimental method

X-RAY DIFFRACTION (3.1 Å)