6LUS

Crystal structure of the Mengla Virus VP30 C-terminal domain

Summary for 6LUS

• Entry DOI: 10.2210/pdb6lus/pdb
• Descriptor: Minor nucleoprotein VP30 (2 entities in total)
• Functional Keywords: vp30, viral protein
• Biological source: Mengla dianlovirus
• Total number of polymer chains: 1
• Total formula weight: 14742.69

Authors

Dong, S.S.,Wen, K.N.,Chu, H.G.,Wang, C.H.,Qin, X.C. (deposition date: 2020-01-30, release date: 2020-12-02, Last modification date: 2023-11-29)

Primary citation

Dong, S.,Wen, K.,Chu, H.,Li, H.,Yu, Q.,Wang, C.,Qin, X.
Crystal structure of the Mengla virus VP30 C-terminal domain.
Biochem.Biophys.Res.Commun., 525:392-397, 2020

PubMed Abstract: The family Filoviridae contains many important human viruses, including Marburg virus (MARV) and Ebola virus (EBOV). Měnglà virus (MLAV), a newly discovered filovirus, is considered a potential human pathogen. The VP30 C-terminal domain (CTD) of these filoviruses plays an essential role in virion assembly. In common with other filoviruses, MLAV VP30 CTD mainly exists as a dimer in solution. In this work, we determined the crystal structure of recombinant MLAV VP30 CTD monomer, verifying that C-terminal helix-7 (H7) is critical for the dimerization process. This study provides a preliminary model for investigation of MLAV VP30 CTD as an anti-filovirus drug development target.

PubMed: 32093889
DOI: 10.1016/j.bbrc.2020.02.089

Experimental method

X-RAY DIFFRACTION (1.4 Å)