5YPS

The structural basis of histone chaperoneVps75

Summary for 5YPS

• Entry DOI: 10.2210/pdb5yps/pdb
• Descriptor: Vacuolar protein sorting-associated protein 75, CALCIUM ION, PENTAETHYLENE GLYCOL, ... (7 entities in total)
• Functional Keywords: histone chaperone, acetylation, chaperone
• Biological source: Pneumocystis carinii B80 (Rat pneumocystis pneumonia agent)
• Total number of polymer chains: 6
• Total formula weight: 183182.49

Authors

Chen, Y.,Zhang, Y.,Dou, Y.,Wang, M.,Xu, S.,Jiang, H.,Limper, A.,Su, D. (deposition date: 2017-11-03, release date: 2018-11-07, Last modification date: 2020-06-10)

• Primary citation: Chen, Y.,Zhang, Y.,Ye, H.,Dou, Y.,Lu, D.,Li, X.,Limper, A.H.,Hua, J.,Su, D.; Structural basis for the acetylation of histone H3K9 and H3K27 mediated by the histone chaperone Vps75 inPneumocystis carinii.; Signal Transduct Target Ther, 4:14-14, 2019; PubMed: 31098304; DOI: 10.1038/s41392-019-0047-8

Experimental method

X-RAY DIFFRACTION (2.097 Å)