PDBsum entry: 2c6s

Virus/viral protein

PDB id: 2c6s

Contents

Protein chains

(+ 9 more) 444 a.a. *

* Residue conservation analysis

PDB id:

2c6s

Name:

Virus/viral protein

Title:

Human adenovirus penton base 2 12 chimera

Structure:

Adenovirus 2,12 penton base chimera. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o. Fragment: residues 49-571. Synonym: penton protein. Engineered: yes. Other_details: hypervariable loop of human adenovirus 2 penton base replaced with hypervariable loop of human adenovirus 12

Source:

Human adenovirus c. Organism_taxid: 10515. Strain: serotype 2. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_cell_line: high five.

Resolution:

3.60Å R-factor: 0.276 R-free: 0.340

Authors:

C.Zubieta,L.Blanchoin,S.Cusack

Key ref:

C.Zubieta et al. (2006). Structural and biochemical characterization of a human adenovirus 2/12 penton base chimera. FEBS J, 273, 4336-4345. PubMed id: 16939624 DOI: 10.1111/j.1742-4658.2006.05430.x

Date:

11-Nov-05 Release date: 06-Sep-06

Protein chains

P03276  (PEN3_ADE02) -  Penton protein

Seq: 571 a.a.

Struc: 444 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 

• Biological process: interspecies interaction between organisms (1 term)
• Biochemical function: structural molecule activity (1 term)

DOI no: 10.1111/j.1742-4658.2006.05430.x

FEBS J 273:4336-4345 (2006)

PubMed id: 16939624

Structural and biochemical characterization of a human adenovirus 2/12 penton base chimera.

C.Zubieta, L.Blanchoin, S.Cusack.

ABSTRACT

The vertex of the adenoviral capsid is formed by the penton, a complex of two proteins, the pentameric penton base and the trimeric fiber protein. The penton contains all necessary components for viral attachment and entry into the host cell. After initial attachment via the head domain of the fiber protein, the penton base interacts with cellular integrins through an Arg-Gly-Asp (RGD) motif located in a hypervariable surface loop, triggering virus internalization. In order to investigate the structural and functional role of this region, we replaced the hypervariable loop of serotype 2 with the corresponding, but much shorter, loop of serotype 12 and compared it to the wild type. Here, we report the 3.6 A crystal structure of a human adenovirus 2/12 penton base chimera crystallized as a dodecamer. The structure is generally similar to human adenovirus 2 penton base, with the main differences localized to the fiber protein-binding site. Fluorescence anisotropy assays using a trimeric fiber protein mimetic called the minifiber and wild-type human adenovirus 2 and chimeric penton base demonstrate that fiber protein binding is independent of the hypervariable loop, with a K(d) for fiber binding estimated in the 1-2 microm range. Interestingly, competition assays using labeled and unlabeled minifiber demonstrated virtually irreversible binding to the penton base, which we ascribe to a conformational change, on the basis of comparisons of all available penton base structures.

Selected figure(s)

Figure 2.
Fig. 2. Oligomerization of hAd2/12 penton base. (A) Monomer, pentamer, and dodecamer. The orientation of the monomer in red is kept throughout. (B) Asymmetric unit consisting of three pentamers (left) and the full dodecamer formed by the space group symmetry (right). The pentamers in the asymmetric unit are in red.

Figure 4.
Fig. 4. Comparison of the hAd2, hAd2/12 and hAd2–fiber peptide complex structures. (A) Stereo overlay of hAd2 penton base (yellow), hAd2/12 (blue) and hAd2 fiber peptide complex (pink). The hAd2 monomers are partially transparent, for clarity. The gray box outlines helix 7. (B) Stereo overlay of helix 7 with hAd2 penton base (yellow), hAd2/12 (blue), and hAd2 fiber peptide complex (pink). The fiber peptide is drawn as ball-and-stick and colored by atom.

The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS J (2006, 273, 4336-4345) copyright 2006.

Figures were selected by an automated process.