3JB8

Insight into Three-dimensional structure of Maize Chlorotic Mottle Virus Revealed by Single Particle Analysis

Summary for 3JB8

• Entry DOI: 10.2210/pdb3jb8/pdb
• EMDB information: 6382
• Descriptor: Coat protein (1 entity in total)
• Functional Keywords: mcmv, single particle analysis, three-dimensional structure, icosahedral virus, transmission, virus
• Biological source: Maize chlorotic mottle virus (MCMV)
• Total number of polymer chains: 3
• Total formula weight: 58963.89

Authors

Wang, C.Y.,Zhang, Q.F.,Gao, Y.Z.,Zhou, X.P.,Ji, G.,Huang, X.J.,Hong, J.,Zhang, C.X. (deposition date: 2015-08-04, release date: 2016-07-13, Last modification date: 2024-03-20)

Primary citation

Wang, C.Y.,Zhang, Q.F.,Gao, Y.Z.,Zhou, X.P.,Ji, G.,Huang, X.J.,Hong, J.,Zhang, C.X.
Insight into the three-dimensional structure of maize chlorotic mottle virus revealed by Cryo-EM single particle analysis.
Virology, 485:171-178, 2015

PubMed Abstract: Maize chlorotic mottle virus (MCMV) is the only member of the Machlomovirus genus in the family Tombusviridae. Here, we obtained the Cryo-EM structure of MCMV by single particle analysis with most local resolution at approximately 4 Å. The Cα backbone was built based on residues with bulky side chains. The resolved C-terminus of the capsid protein subunit and obvious openings at the 2-fold axis demonstrated the compactness of the asymmetric unit, which indicates an important role in the stability of MCMV. The Asp116 residue from each subunit around the 5-fold and 3-fold axes contributed to the negative charges in the centers of the pentamers and hexamers, which might serve as a solid barrier against the leakage of genomic RNA. Finally, the loops most exposed on the surface were analyzed and are proposed to be potential functional sites related to MCMV transmission.

PubMed: 26275511
DOI: 10.1016/j.virol.2015.07.014

Experimental method

ELECTRON MICROSCOPY (3.6 Å)