PDBsum entry 1v1i

Adenovirus

PDB id: 1v1i

Contents

Protein chains

102 a.a. *

Waters ×237

* Residue conservation analysis

PDB id:

1v1i

Name:

Adenovirus

Title:

Adenovirus fibre shaft sequence n-terminally fused to the bacteriophage t4 fibritin foldon trimerisation motif with a long linker

Structure:

Fibritin, fiber protein. Chain: a, b, c. Fragment: shaft domain plus foldon domain, residues 319-392 and 457- 483. Synonym: artifical fusion of adenovirus fibre shaft with bacteriophage t4 fibritin foldon, whisker antigen control protein, collar protein. Engineered: yes. Other_details: artificial fusion protein of adenovirus type 2 fibre

Source:

Human adenovirus c, enterobacteria phage t4. Organism_taxid: 129951, 10665. Atcc: vr-846 and 11303-b4. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Trimer (from PDB file)

Resolution:

1.90Å R-factor: 0.232 R-free: 0.283

Authors:

K.Papanikolopoulou,S.Teixeira,H.Belrhali,V.T.Forsyth,A.Mitraki, M.J.Van Raaij

Key ref:

K.Papanikolopoulou et al. (2004). Adenovirus fibre shaft sequences fold into the native triple beta-spiral fold when N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif. J Mol Biol, 342, 219-227. PubMed id: 15313619 DOI: 10.1016/j.jmb.2004.07.008

Date:

16-Apr-04 Release date: 30-Jul-04

Protein chains

P03275  (SPIKE_ADE02) -  Fiber protein from Human adenovirus C serotype 2

Seq: 582 a.a.

Struc: 102 a.a.*

Protein chains

P10104  (WAC_BPT4) -  Fibritin from Enterobacteria phage T4

Seq: 487 a.a.

Struc: 102 a.a.*

* PDB and UniProt seqs differ at 82 residue positions (black crosses)

DOI no: 10.1016/j.jmb.2004.07.008

J Mol Biol 342:219-227 (2004)

PubMed id: 15313619

Adenovirus fibre shaft sequences fold into the native triple beta-spiral fold when N-terminally fused to the bacteriophage T4 fibritin foldon trimerisation motif.

K.Papanikolopoulou, S.Teixeira, H.Belrhali, V.T.Forsyth, A.Mitraki, M.J.van Raaij.

ABSTRACT

Adenovirus fibres are trimeric proteins that consist of a globular C-terminal domain, a central fibrous shaft and an N-terminal part that attaches to the viral capsid. In the presence of the globular C-terminal domain, which is necessary for correct trimerisation, the shaft segment adopts a triple beta-spiral conformation. We have replaced the head of the fibre by the trimerisation domain of the bacteriophage T4 fibritin, the foldon. Two different fusion constructs were made and crystallised, one with an eight amino acid residue linker and one with a linker of only two residues. X-ray crystallographic studies of both fusion proteins shows that residues 319-391 of the adenovirus type 2 fibre shaft fold into a triple beta-spiral fold indistinguishable from the native structure, although this is now resolved at a higher resolution of 1.9 A. The foldon residues 458-483 also adopt their natural structure. The intervening linkers are not well ordered in the crystal structures. This work shows that the shaft sequences retain their capacity to fold into their native beta-spiral fibrous fold when fused to a foreign C-terminal trimerisation motif. It provides a structural basis to artificially trimerise longer adenovirus shaft segments and segments from other trimeric beta-structured fibre proteins. Such artificial fibrous constructs, amenable to crystallisation and solution studies, can offer tractable model systems for the study of beta-fibrous structure. They can also prove useful for gene therapy and fibre engineering applications.

Selected figure(s)

Figure 2.
Figure 2. Space-filling models of the long-linker (a) and short-linker (b) adenovirus fibre shaft-fibritin foldon chimeras in the same orientation as Figure 1.

Figure 3.
Figure 3. Ribbon diagrams of the long-linker (a) and short-linker (b) adenovirus fibre shaft-fibritin foldon chimeras in the same orientation as Figure 1. The N and the C termini in the A subunits are labelled.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2004, 342, 219-227) copyright 2004.

Figures were selected by the author.

Author's comment

Two structures of a fragment of the human adenovirus type fibre shaft domain artifically trimerised by the bacteriophage T4 fibritin foldon domain. Two structure were solved, one in which the domains were joined by a long linker (invisible in the structure) and one with a short linker (partially visible). The structure proves the fibre shaft domain maintain the same fold and suggests strategies for structure solution strategies of other fibre shaft domains.
Mark J. van Raaij