5H0R

RNA dependent RNA polymerase ,vp4,dsRNA

Summary for 5H0R

• Entry DOI: 10.2210/pdb5h0r/pdb
• Related: 5H0S
• EMDB information: 9564 9565
• Descriptor: RNA-dependent RNA polymerase, VP4 protein, RNA (42-MER), ... (4 entities in total)
• Functional Keywords: structural classification, transferase-rna complex, transferase/rna
• Biological source: Bombyx mori cytoplasmic polyhedrosis virus (BmCPV); More
• Total number of polymer chains: 4
• Total formula weight: 229407.67

Authors

Li, X.,Zhou, N.,Chen, W.,Zhu, B.,Wang, X.,Xu, B.,Wang, J.,Liu, H.,Cheng, L. (deposition date: 2016-10-06, release date: 2017-01-25, Last modification date: 2024-03-27)

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 (3.9 Å)