PDBsum entry 2cse

Virus

PDB id: 2cse

Contents

Protein chains

(+ 4 more) 641 a.a.* *

(+ 4 more) 365 a.a.* *

1284 a.a.* *

1031 a.a.* *

1221 a.a.* *

417 a.a.* *

1264 a.a.* *

* Residue conservation analysis

* C-alpha coords only

PDB id:

2cse

Name:

Virus

Title:

Features of reovirus outer-capsid protein mu1 revealed by electron and image reconstruction of the virion at 7.0-a resolution

Structure:

Major outer-capsid protein mu1. Chain: a, b, c, p, q, r, j, k, l, t. Major capsid surface protein sigma-3. Chain: s, d, e, f, m, n, o, g, h, i. Guanylyltransferase. Chain: u. Major core protein lambda 1. Chain: v, w. Sigma 2 protein.

Source:

Mammalian orthoreovirus 1. Organism_taxid: 10884. Strain: lang. Mammalian orthoreovirus 3. Organism_taxid: 10886. Strain: dearing. Strain: lang

Authors:

X.Zhang,Y.Ji,L.Zhang,S.C.Harrison,D.C.Marinescu,M.L.Nibert,T.S.Baker

Key ref:

X.Zhang et al. (2005). Features of reovirus outer capsid protein mu1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0 Angstrom resolution. Structure, 13, 1545-1557. PubMed id: 16216585 DOI: 10.1016/j.str.2005.07.012

Date:

21-May-05 Release date: 18-Oct-05

Protein chains

P11077  (MU1_REOVL) -  Outer capsid protein mu-1 from Reovirus type 1 (strain Lang)

Seq: 708 a.a.

Struc: 641 a.a.*

Protein chains

P07939  (SIGM3_REOVL) -  Outer capsid protein sigma-3 from Reovirus type 1 (strain Lang)

Seq: 365 a.a.

Struc: 365 a.a.*

Protein chain

P11079  (LMBD2_REOVD) -  Outer capsid protein lambda-2 from Reovirus type 3 (strain Dearing)

Seq: 1289 a.a.

Struc: 1284 a.a.

Protein chain

Q9WAB2  (LMBD1_REOVL) -  Inner capsid protein lambda-1 from Reovirus type 1 (strain Lang)

Seq: 1275 a.a.

Struc: 1031 a.a.

Protein chain

Q9WAB2  (LMBD1_REOVL) -  Inner capsid protein lambda-1 from Reovirus type 1 (strain Lang)

Seq: 1275 a.a.

Struc: 1221 a.a.

Protein chains

P11314  (SIGM2_REOVL) -  Inner capsid protein sigma-2 from Reovirus type 1 (strain Lang)

Seq: 418 a.a.

Struc: 417 a.a.

Protein chain

P0CK32  (RDRP_REOVL) -  RNA-directed RNA polymerase lambda-3 from Reovirus type 1 (strain Lang)

Seq: 1267 a.a.

Struc: 1264 a.a.

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class 2: Chain 1: E.C.2.7.7.48 - RNA-directed Rna polymerase.
• Reaction: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
• Enzyme class 3: Chain U: E.C.2.1.1.56 - mRNA (guanine-N(7))-methyltransferase.
• Reaction: a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L- methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
• Enzyme class 4: Chain U: E.C.2.7.7.50 - mRNA guanylyltransferase.
• Reaction: a 5'-end diphospho-ribonucleoside in mRNA + GTP + H⁺ = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate
• Enzyme class 5: Chains V, W: E.C.3.6.4.13 - Rna helicase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1016/j.str.2005.07.012

Structure 13:1545-1557 (2005)

PubMed id: 16216585

Features of reovirus outer capsid protein mu1 revealed by electron cryomicroscopy and image reconstruction of the virion at 7.0 Angstrom resolution.

X.Zhang, Y.Ji, L.Zhang, S.C.Harrison, D.C.Marinescu, M.L.Nibert, T.S.Baker.

ABSTRACT

Reovirus is a useful model for addressing the molecular basis of membrane penetration by one of the larger nonenveloped animal viruses. We now report the structure of the reovirus virion at approximately 7.0 A resolution as obtained by electron cryomicroscopy and three-dimensional image reconstruction. Several features of the myristoylated outer capsid protein mu1, not seen in a previous X-ray crystal structure of the mu1-sigma3 heterohexamer, are evident in the virion. These features appear to be important for stabilizing the outer capsid, regulating the conformational changes in mu1 that accompany perforation of target membranes, and contributing directly to membrane penetration during cell entry.

Selected figure(s)

Figure 6.
Figure 6. Cryo-EM Densities for Residues 72-96 in the Averaged µ1 Cryo-EM Map
(A) Close-up stereo view of a region near the base of two adjacent µ1 trimers, looking toward the virion interior. Cryo-EM densities (gray net, contoured at 2.0 s) are fitted with the X-ray crystal models of two µ1 trimers (light-blue and brown ribbon traces, respectively). Extra cryo-EM densities forming a U-shaped loop (green net) were assigned to residues 72-96. Black and blue spheres, abutting the two ends of the U-shaped densities, identify the positions of residues Ile71 and Asp97, respectively, in the light-blue subunit. A short a helix (residues 122-127), colored purple in the otherwise brown subunit, is slightly displaced from the attributed cryo-EM densities, apparently owing to contacts with the 72-96 loop.
(B) Same as shown in (A), but with a tentative ribbon trace (magenta), including an a helix, built into the extra cryo-EM densities ascribed to residues 72-96.
(C) Same as shown in (B), but viewed in an orthogonal direction, from the left side of (B) to illustrate apparent interactions between the 72-96 (magenta) and the 51-62 (cyan) loops. The 51-62 loop is clearly displaced from the associated cryo-EM densities. A b strand formed by residues 63-65 (black) also contacts the 72-96 loop. The 10 Å scale bar also applies to (A) and (B).
(D) Bottom view (from virion interior) of two adjacent µ1 trimers (light-blue and brown) in the atomic model. Putative traces for the two 72-96 loops at the trimer-trimer interface are shown in magenta. The scale bar is 25 Å.

The above figure is reprinted by permission from Cell Press: Structure (2005, 13, 1545-1557) copyright 2005.

Figure was selected by an automated process.