PDBsum entry 5i2s

Viral protein

PDB id: 5i2s

Contents

Protein chain

413 a.a.

Ligands

NAG-NAG

NAG

Metals

_YB ×2

PDB id:

5i2s

Name:

Viral protein

Title:

Prefusion form of the vesicular stomatitis virus glycoprotein g ectodomain

Structure:

Glycoprotein g. Chain: a

Source:

Vesicular stomatitis indiana virus (strain mudd-summers). Vsiv. Organism_taxid: 11279. Strain: mudd-summers

Resolution:

3.00Å R-factor: 0.184 R-free: 0.240

Authors:

S.Roche,S.Bressanelli

Key ref:

S.Roche et al. (2007). Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G. Science, 315, 843-848. PubMed id: 17289996 DOI: 10.1126/science.1135710

Date:

09-Feb-16 Release date: 02-Mar-16

Supersedes:

2j6j

Protein chain

P0C2X0  (VGLG_VSIVM) -  Glycoprotein G (Fragment) from Vesicular stomatitis Indiana virus (strain Mudd-Summers)

Seq: 423 a.a.

Struc: 413 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1126/science.1135710

Science 315:843-848 (2007)

PubMed id: 17289996

Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G.

S.Roche, F.A.Rey, Y.Gaudin, S.Bressanelli.

ABSTRACT

Glycoprotein G of the vesicular stomatitis virus triggers membrane fusion via a low pH-induced structural rearrangement. Despite the equilibrium between the pre- and postfusion states, the structure of the prefusion form, determined to 3.0 angstrom resolution, shows that the fusogenic transition entails an extensive structural reorganization of G. Comparison with the structure of the postfusion form suggests a pathway for the conformational change. In the prefusion form, G has the shape of a tripod with the fusion loops exposed, which point toward the viral membrane, and with the antigenic sites located at the distal end of the molecule. A large number of G glycoproteins, perhaps organized as in the crystals, act cooperatively to induce membrane merging.

Selected figure(s)

Figure 2.
Fig. 2. Structural changes in the protomer between the pre- and postfusion conformations and relative movements of domains. In (A) and (B), fragments of the pre- and postfusion conformations are displayed to the left and right, respectively. Secondary structure elements of the prefusion form that refold are named and numbered according to fig. S2. (A) Relative movement of PH (DIII, orange) and fusion (DIV, yellow) domains. The protomers are superimposed on DIII. Hinge residues 47 to 52 (prefusion helix A^0) and 173 to 180 (postfusion helix C) are colored in cyan and gray-blue, respectively. (B) Domain II refolding. DI and DIII are omitted in the top panels for clarity but are shown in the bottom panels to provide the relative orientations in the two forms. The protomers are superimposed on the invariant part of DII, which is indicated in dark blue, whereas the three segments that refold and/or relocate are indicated in shades of green. In the prefusion form, strands a^1 and y^1 form an interchain ß sheet. The DIII-DIV hinge (bottom panels) is displayed and colored as in (A), with the two segments connected by a yellow bar to mark the location of the fusion domain. (C) Cartoon representation of the relative organization of domains with respect to the viral membrane during the conformational change. The one-sided black arrows indicate the relative movements of domains. The N- to C-terminal orientations of helices F2 (blue; left), F (blue; middle and right), and H (dark blue; right) are indicated with white arrows. Pre- (left) and postfusion (right) conformations are shown. The trimer axes are indicated. The middle cartoon shows how the fusion loops (in green) would be projected after the refolding of both the DIII-DIV hinge and the DII-DIII connection and before the C-terminal refolding of helix H.

Figure 5.
Fig. 5. Antigenic sites of Rhabdoviridae mapped onto the surface of the pre- (A) and postfusion (B) VSV G trimers. Sites are colored on both forms and labeled on the form(s) in which they are recognized. VSV sites are labeled in bold, and RV sites are labeled in italics within parentheses. VSV sites A1 (residues 37 to 38, corresponding to RV antigenic site II located on segments composed of residues 34 to 42 and 198 to 200) and A2 (located at the surface of helix E indicated in Fig. 1) are indicated in shades of red. The RV G site recognized by antibody 17D2 (between residues 255 and 270) is in orange. NS (extending from amino acid 10 to 15) is in dark blue. VSV site B (extending from amino acid 341 to 347), corresponding to RV G minor antigenic site a (amino acid 340 to 342), is in magenta. In the prefusion conformation, the cleft between DI and DIII is colored black. It is flanked by residues 331 and 334, in gray, whose counterparts in RV affect virulence.

The above figures are reprinted by permission from the AAAs: Science (2007, 315, 843-848) copyright 2007.

Figures were selected by the author.