PDBsum entry: 1faf

Viral protein

PDB id: 1faf

Contents

Protein chain

79 a.a.

PDB id:

1faf

Name:

Viral protein

Title:

Nmr structure of the n-terminal j domain of murine polyomavirus t antigens.

Structure:

Large t antigen. Chain: a. Fragment: n-terminal domain. Engineered: yes

Source:

Murine polyomavirus. Organism_taxid: 10634. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

47 models

Authors:

M.V.Berjanskii,M.I.Riley,A.Xie,V.Semenchenko,W.R.Folk, S.R.Van Doren

Key ref:

M.V.Berjanskii et al. (2000). NMR structure of the N-terminal J domain of murine polyomavirus T antigens. Implications for DnaJ-like domains and for mutations of T antigens. J Biol Chem, 275, 36094-36103. PubMed id: 10950962 DOI: 10.1074/jbc.M006572200

Date:

13-Jul-00 Release date: 22-Nov-00

Protein chain

P03074  (LT_POVM3) -  Large T antigen

Seq: 782 a.a.

Struc: 79 a.a.

 Gene Ontology (GO) functional annotation 

• Biochemical function: heat shock protein binding (1 term)

DOI no: 10.1074/jbc.M006572200

J Biol Chem 275:36094-36103 (2000)

PubMed id: 10950962

NMR structure of the N-terminal J domain of murine polyomavirus T antigens. Implications for DnaJ-like domains and for mutations of T antigens.

M.V.Berjanskii, M.I.Riley, A.Xie, V.Semenchenko, W.R.Folk, S.R.Van Doren.

ABSTRACT

The NMR structure of the N-terminal, DnaJ-like domain of murine polyomavirus tumor antigens (PyJ) has been determined to high precision, with root mean square deviations to the mean structure of 0.38 A for backbone atoms and 0.94 A for all heavy atoms of ordered residues 5-41 and 50-69. PyJ possesses a three-helix fold, in which anti-parallel helices II and III are bridged by helix I, similar to the four-helix fold of the J domains of DnaJ and human DnaJ-1. PyJ differs significantly in the lengths of N terminus, helix I, and helix III. The universally conserved HPD motif appears to form a His-Pro C-cap of helix II. Helix I features a stabilizing Schellman C-cap that is probably conserved universally among J domains. On the helix II surface where positive charges of other J domains have been implicated in binding of hsp70s, PyJ contains glutamine residues. Nonetheless, chimeras that replace the J domain of DnaJ with PyJ function like wild-type DnaJ in promoting growth of Escherichia coli. This activity can be modulated by mutations of at least one of these glutamines. T antigen mutations reported to impair cellular transformation by the virus, presumably via interactions with PP2A, cluster in the hydrophobic folding core and at the extreme N terminus, remote from the HPD loop.

Selected figure(s)

Figure 4.
Fig. 4. Stacking of His-42 and Pro-43 side chains and hydrogen bonding of His-42 with Lys-45 in PyJ. Side chains are colored as follows: His-42 in violet, Pro-43 in green, and Asp-44 in red. Locations of helices II and III are indicated. The hydrogen bond between the backbone amide (cyan) of Lys-45 and the carbonyl (orange) of His-42 is colored yellow.

Figure 5.
Fig. 5. Surface of helix II face of PyJ (A), HDJ-1 J domain (B), and overlay of NMR ensembles of PyJ and HDJ-1-(1-77) (C). A and B, helix II is in the foreground. The accessible surface is colored such that positively charged residues are blue, negatively charged residues are red, glutamine and asparagine are violet, and hydrophobic residues are green. The surface plots of representative NMR models (number 22 of PyJ ensemble and number 10 of HDJ-1 ensemble) were created with GRASP (55). C, the ensembles are rotated relative to views (a and b) by approximately 60° about the axis vertical within the plane of the page. The PyJ backbone is colored in black. HDJ-1 (residues 1-77) is shown in violet. To overlay ensembles, PyJ residues 7-10, 13-17, 19-23, 26-43, 48-63, and 65-68 were fitted to HDJ-1 residues 1-4, 5-9, 10-14, 15-32, 40-55, and 56-59, chosen by the alignment obtained from the Dali server (68). Side chains of positively charged residues of helix II in HDJ-1 and of corresponding residues of PyJ are displayed. Side chains are colored as follows: Lys-20, Arg-21, Arg-24, Arg-25, and Lys-34 of HDJ-1, blue; Gln-31, Gln-32, and Gln-36 of PyJ, green; Lys-35 and Lys-45 of PyJ, gold.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2000, 275, 36094-36103) copyright 2000.

Figures were selected by an automated process.