5H0S

EM Structure of VP1A and VP1B

Summary for 5H0S

• Entry DOI: 10.2210/pdb5h0s/pdb
• Related: 5H0R
• EMDB information: 9564 9565
• Descriptor: VP1 (1 entity in total)
• Functional Keywords: structural classification, transferase
• Biological source: Bombyx mori cypovirus 1 (BmCPV)
• Total number of polymer chains: 2
• Total formula weight: 297392.12

Authors

Li, X.,Zhou, N.,Xu, B.,Chen, W.,Zhu, B.,Wang, X.,Wang, J.,Liu, H.,Cheng, L. (deposition date: 2016-10-06, release date: 2017-01-25, Last modification date: 2024-10-16)

Primary citation

Li, X.,Zhou, N.,Chen, W.,Zhu, B.,Wang, X.,Xu, B.,Wang, J.,Liu, H.,Cheng, L.
Near-Atomic Resolution Structure Determination of a Cypovirus Capsid and Polymerase Complex Using Cryo-EM at 200kV
J. Mol. Biol., 429:79-87, 2017

PubMed Abstract: Single-particle cryo-electron microscopy (cryo-EM) allows the high-resolution structural determination of biological assemblies in a near-native environment. However, all high-resolution (better than 3.5Å) cryo-EM structures reported to date were obtained by using 300kV transmission electron microscopes (TEMs). We report here the structures of a cypovirus capsid of 750-Å diameter at 3.3-Å resolution and of RNA-dependent RNA polymerase (RdRp) complexes within the capsid at 3.9-Å resolution using a 200-kV TEM. The newly resolved structure revealed conformational changes of two subdomains in the RdRp. These conformational changes, which were involved in RdRp's switch from non-transcribing to transcribing mode, suggest that the RdRp may facilitate the unwinding of genomic double-stranded RNA. The possibility of 3-Å resolution structural determinations for biological assemblies of relatively small sizes using cryo-EM at 200kV was discussed.

PubMed: 27914893
DOI: 10.1016/j.jmb.2016.11.025

Experimental method

ELECTRON MICROSCOPY (3.3 Å)