3VCB

C425S mutant of the C-terminal cytoplasmic domain of non-structural protein 4 from mouse hepatitis virus A59

Summary for 3VCB

• Entry DOI: 10.2210/pdb3vcb/pdb
• Descriptor: RNA-directed RNA polymerase (2 entities in total)
• Functional Keywords: new fold; homodimer, host membrane; multi-pass membrane protein, cytoplasmic, hydrolase, viral protein
• Biological source: Murine hepatitis virus
• Cellular location: Host cytoplasm, host perinuclear region (By similarity). Host membrane; Multi-pass membrane protein (By similarity): Q9J3E9
• Total number of polymer chains: 2
• Total formula weight: 21169.71

Authors

Xu, X.,Lou, Z.,Ma, Y.,Chen, X.,Yang, Z.,Tong, X.,Zhao, Q.,Xu, Y.,Deng, H.,Bartlam, M.,Rao, Z. (deposition date: 2012-01-03, release date: 2012-01-11, Last modification date: 2024-02-28)

Primary citation

Xu, X.,Lou, Z.,Ma, Y.,Chen, X.,Yang, Z.,Tong, X.,Zhao, Q.,Xu, Y.,Deng, H.,Bartlam, M.,Rao, Z.
Crystal structure of the C-terminal cytoplasmic domain of non-structural protein 4 from mouse hepatitis virus A59.
Plos One, 4:e6217-e6217, 2009

PubMed Abstract: The replication of coronaviruses takes place on cytoplasmic double membrane vesicles (DMVs) originating in the endoplasmic reticulum (ER). Three trans-membrane non-structural proteins, nsp3, nsp4 and nsp6, are understood to be membrane anchors of the coronavirus replication complex. Nsp4 is localized to the ER membrane when expressed alone but is recruited into the replication complex in infected cells. It is revealed to contain four trans-membrane regions and its N- and C-termini are exposed to the cytosol.

PubMed: 19593433
DOI: 10.1371/journal.pone.0006217

Experimental method

X-RAY DIFFRACTION (2.4 Å)