PDBsum entry 1dto

Viral protein

PDB id: 1dto

Contents

Protein chain

200 a.a. *

Waters ×211

* Residue conservation analysis

PDB id:

1dto

Name:

Viral protein

Title:

Crystal structure of the complete transactivation domain of e2 protein from the human papillomavirus type 16

Structure:

Regulatory protein e2. Chain: a. Fragment: transactivation domain. Engineered: yes

Source:

Human papillomavirus type 16. Organism_taxid: 333760. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PDB file)

Resolution:

1.90Å R-factor: 0.236 R-free: 0.305

Authors:

A.A.Antson,J.E.Burns,O.V.Moroz,D.J.Scott,C.M.Sanders,I.B.Bronstein, G.G.Dodson,K.S.Wilson,N.Maitland

Key ref:

A.A.Antson et al. (2000). Structure of the intact transactivation domain of the human papillomavirus E2 protein. Nature, 403, 805-809. PubMed id: 10693813 DOI: 10.1038/35001638

Date:

13-Jan-00 Release date: 23-Feb-00

Protein chain

P03120  (VE2_HPV16) -  Regulatory protein E2 from Human papillomavirus type 16

Seq: 365 a.a.

Struc: 200 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1038/35001638

Nature 403:805-809 (2000)

PubMed id: 10693813

Structure of the intact transactivation domain of the human papillomavirus E2 protein.

A.A.Antson, J.E.Burns, O.V.Moroz, D.J.Scott, C.M.Sanders, I.B.Bronstein, G.G.Dodson, K.S.Wilson, N.J.Maitland.

ABSTRACT

Papillomaviruses cause warts and proliferative lesions in skin and other epithelia. In a minority of papillomavirus types ('high risk, including human papillomaviruses 16, 18, 31, 33, 45 and 56), further transformation of the wart lesions can produce tumours. The papillomavirus E2 protein controls primary transcription and replication of the viral genome. Both activities are governed by a approximately 200 amino-acid amino-terminal module (E2NT) which is connected to a DNA-binding carboxy-terminal module by a flexible linker. Here we describe the crystal structure of the complete E2NT module from human papillomavirus 16. The E2NT module forms a dimer both in the crystal and in solution. Amino acids that are necessary for transactivation are located at the dimer interface, indicating that the dimer structure may be important in the interactions of E2NT with viral and cellular transcription factors. We propose that dimer formation may contribute to the stabilization of DNA loops which may serve to relocate distal DNA-binding transcription factors to the site of human papillomavirus transcription initiation.

Selected figure(s)

Figure 1.
Figure 1: Functional and structural assignments of papillomavirus E2. View of the N-terminal, linker and C-terminal modules indicating the known functions of each. Amino-acid numbers that delimit the modules correspond to those of HPV16 E2.

Figure 3.
Figure 3: Structural features of E2. a, Stereo view of the electron density with the final model, at the dimer interface of the E2NT module, viewed down the crystallographic twofold axis. The likelihood weighted 2|F[o]|-| F[c]| electron density map is contoured at the 1.5 level. Ribbons of two independent monomers are shown in aquamarine and yellow. Side chains of Arg 37 and Ile 73, which are known to be critical for transactivation2, 10, are shown in dark green; side chains of other residues at the dimer interface are shown in light green. Oxygen atoms are in red, nitrogen atoms in blue; water molecules are shown as orange spheres and hydrogen bonds as dashed sticks. b, Stereo ribbon diagram of the E2NT dimer, showing the extent of the interface between the two subunits. The view is as in a but rotated clockwise by 90 °. Side chains of Gln 12 and Glu 39 that are critical for interactions with E1 (refs 2,10,18) are shown in magenta. Side chains of residues at the dimer interface are coloured as in a.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (2000, 403, 805-809) copyright 2000.

Figures were selected by an automated process.