5I2M

CRYSTAL STRUCTURE OF VSV-INDIANA (MUDD-SUMMERS STRAIN) GLYCOPROTEIN UNDER ITS ACIDIC CONFORMATION

Replaces:  2CMZ

Summary for 5I2M

• Entry DOI: 10.2210/pdb5i2m/pdb
• Descriptor: Glycoprotein G, 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: membrane, lipoprotein, glycoprotein, transmembrane, envelope protein, membrane protein
• Biological source: Vesicular stomatitis Indiana virus (strain Mudd-Summers) (VSIV)
• Cellular location: Virion membrane ; Single-pass type I membrane protein : P0C2X0
• Total number of polymer chains: 3
• Total formula weight: 143838.38

Authors

Roche, S.,Bressanelli, S. (deposition date: 2016-02-09, release date: 2016-02-24, Last modification date: 2024-11-20)

Primary citation

Roche, S.,Bressanelli, S.,Rey, F.A.,Gaudin, Y.
Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G.
Science, 313:187-191, 2006

PubMed Abstract: The vesicular stomatitis virus has an atypical membrane fusion glycoprotein (G) exhibiting a pH-dependent equilibrium between two forms at the virus surface. Membrane fusion is triggered during the transition from the high- to low-pH form. The structure of G in its low-pH form shows the classic hairpin conformation observed in all other fusion proteins in their postfusion conformation, in spite of a novel fold combining features of fusion proteins from classes I and II. The structure provides a framework for understanding the reversibility of the G conformational change. Unexpectedly, G is homologous to gB of herpesviruses, which raises important questions on viral evolution.

PubMed: 16840692
DOI: 10.1126/SCIENCE.1127683

Experimental method

X-RAY DIFFRACTION (2.4 Å)