1LG7

Crystal structure of Vesicular Stomatitis Virus Matrix Protein

Summary for 1LG7

• Entry DOI: 10.2210/pdb1lg7/pdb
• Descriptor: VSV matrix protein (2 entities in total)
• Functional Keywords: virus matrix, viral protein
• Biological source: Vesicular stomatitis virus
• Cellular location: Virion membrane; Peripheral membrane protein: Q8B0H2
• Total number of polymer chains: 1
• Total formula weight: 21011.04

Authors

Gaudier, M.,Gaudin, Y.,Knossow, M. (deposition date: 2002-04-15, release date: 2002-06-19, Last modification date: 2024-11-13)

Primary citation

Gaudier, M.,Gaudin, Y.,Knossow, M.
Crystal structure of vesicular stomatitis virus matrix protein.
EMBO J., 21:2886-2892, 2002

PubMed Abstract: The vesicular stomatitis virus (VSV) matrix protein (M) interacts with cellular membranes, self-associates and plays a major role in virus assembly and budding. We present the crystallographic structure, determined at 1.96 A resolution, of a soluble thermolysin resistant core of VSV M. The fold is a new fold shared by the other vesiculovirus matrix proteins. The structure accounts for the loss of stability of M temperature-sensitive mutants deficient in budding, and reveals a flexible loop protruding from the globular core that is important for self-assembly. Membrane floatation shows that, together with the M lysine-rich N-terminal peptide, a second domain of the protein is involved in membrane binding. Indeed, the structure reveals a hydrophobic surface located close to the hydrophobic loop and surrounded by conserved basic residues that may constitute this domain. Lastly, comparison of the negative-stranded virus matrix proteins with retrovirus Gag proteins suggests that the flexible link between their major membrane binding domain and the rest of the structure is a common feature shared by these proteins involved in budding and virus assembly.

PubMed: 12065402
DOI: 10.1093/emboj/cdf284

Experimental method

X-RAY DIFFRACTION (1.96 Å)