6BDF

2.8 A resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy

Summary for 6BDF

• Entry DOI: 10.2210/pdb6bdf/pdb
• EMDB information: 6287
• Descriptor: Proteasome subunit alpha, Proteasome subunit beta (3 entities in total)
• Functional Keywords: proteasome, hydrolase
• Biological source: Thermoplasma acidophilum; More
• Total number of polymer chains: 28
• Total formula weight: 685989.61

Authors

Campbell, M.G.,Veesler, D.,Cheng, A.,Potter, C.S.,Carragher, B. (deposition date: 2017-10-23, release date: 2017-12-27, Last modification date: 2024-03-13)

Primary citation

Campbell, M.G.,Veesler, D.,Cheng, A.,Potter, C.S.,Carragher, B.
2.8 angstrom resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy.
Elife, 4:-, 2015

PubMed Abstract: Recent developments in detector hardware and image-processing software have revolutionized single particle cryo-electron microscopy (cryoEM) and led to a wave of near-atomic resolution (typically ∼3.3 Å) reconstructions. Reaching resolutions higher than 3 Å is a prerequisite for structure-based drug design and for cryoEM to become widely interesting to pharmaceutical industries. We report here the structure of the 700 kDa Thermoplasma acidophilum 20S proteasome (T20S), determined at 2.8 Å resolution by single-particle cryoEM. The quality of the reconstruction enables identifying the rotameric conformation adopted by some amino-acid side chains (rotamers) and resolving ordered water molecules, in agreement with the expectations for crystal structures at similar resolutions. The results described in this manuscript demonstrate that single particle cryoEM is capable of competing with X-ray crystallography for determination of protein structures of suitable quality for rational drug design.

PubMed: 25760083
DOI: 10.7554/eLife.06380

Experimental method

ELECTRON MICROSCOPY (2.8 Å)