PDBsum entry 3gzt

Virus

PDB id: 3gzt

Contents

Protein chains

(+ 7 more) 255 a.a. *

Ligands

NAG-NAG ×13

Metals

_CA ×30

* Residue conservation analysis

PDB id:

3gzt

Name:

Virus

Title:

Vp7 recoated rotavirus dlp

Structure:

Outer capsid glycoprotein vp7. Chain: b, f, g, h, i, j, k, l, m, n, o, p, q. Fragment: vp7 (unp residues 58 to 312)

Source:

Rhesus rotavirus. Rv-a. Organism_taxid: 10969. Strain: uk

Authors:

J.Z.Chen,E.C.Settembre,S.C.Harrison,N.Grigorieff

Key ref:

J.Z.Chen et al. (2009). Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM. Proc Natl Acad Sci U S A, 106, 10644-10648. PubMed id: 19487668 DOI: 10.1073/pnas.0904024106

Date:

07-Apr-09 Release date: 14-Jul-09

Protein chains

P12476  (VP7_ROTRH) -  Outer capsid glycoprotein VP7 from Rotavirus A (strain RVA/Monkey/United States/RRV/1975/G3P5B[3])

Seq: 326 a.a.

Struc: 255 a.a.

DOI no: 10.1073/pnas.0904024106

Proc Natl Acad Sci U S A 106:10644-10648 (2009)

PubMed id: 19487668

Molecular interactions in rotavirus assembly and uncoating seen by high-resolution cryo-EM.

J.Z.Chen, E.C.Settembre, S.T.Aoki, X.Zhang, A.R.Bellamy, P.R.Dormitzer, S.C.Harrison, N.Grigorieff.

ABSTRACT

Rotaviruses, major causes of childhood gastroenteritis, are nonenveloped, icosahedral particles with double-strand RNA genomes. By the use of electron cryomicroscopy and single-particle reconstruction, we have visualized a rotavirus particle comprising the inner capsid coated with the trimeric outer-layer protein, VP7, at a resolution (4 A) comparable with that of X-ray crystallography. We have traced the VP7 polypeptide chain, including parts not seen in its X-ray crystal structure. The 3 well-ordered, 30-residue, N-terminal "arms" of each VP7 trimer grip the underlying trimer of VP6, an inner-capsid protein. Structural differences between free and particle-bound VP7 and between free and VP7-coated inner capsids may regulate mRNA transcription and release. The Ca(2+)-stabilized VP7 intratrimer contact region, which presents important neutralizing epitopes, is unaltered upon capsid binding.

Selected figure(s)

Figure 3.
Interface between 2 VP7 trimers. The interface is shown from the outside of the virus (A) and from the “side”, normal to its symmetry axes (B). The N-terminal arms between residues 58 and 78 are shown as red curves; the approximate positions of the arms between residues 51 (the N terminus) and 57 are shown as dotted green curves, illustrating that the N termini may contribute to intertrimer contacts.

Figure 4.
Conformational differences between DLP and 7RP. The structures of VP2 and VP6 docked into the 7RP cryo-EM density are shown in green whereas the DLP structure (12) is shown in red. A narrowing of the central channel on the icosahedral 5-fold axis and an inward movement of the VP2 and VP6 layers in the 7RP, compared with the DLP, are the principal differences. The VP7 layer of the 7RP is not shown (for clarity); the green arrow indicates the “clamping down” of the VP6 and VP2 layers that accompanies VP7 binding.

Figures were selected by an automated process.