7vf4

Crystal structure of Vps75 from Candida albicans

spinqualitylabelsall models 7vf4, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7vf4 is a 8 chain structure with sequence from Candida albicans SC5314. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: CL, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1D8PT39_CANAL Publication Abstract from PubMed 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 alpha 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. Crystal structure of histone chaperone Vps75 from Candida albicans.,Wang W, Chen X, Yang Z, Chen X, Li C, Wang M Biochem Biophys Res Commun. 2021 Sep 20;578:136-141. doi:, 10.1016/j.bbrc.2021.09.030. PMID:34562653 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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