1FAF

NMR STRUCTURE OF THE N-TERMINAL J DOMAIN OF MURINE POLYOMAVIRUS T ANTIGENS.

1FAF の概要

• エントリーDOI: 10.2210/pdb1faf/pdb
• NMR情報: BMRB: 4738
• 分子名称: LARGE T ANTIGEN (1 entity in total)
• 機能のキーワード: j domain, hpd motif, anti-parallel hairpin of helices, viral protein
• 由来する生物種: Murine polyomavirus
• 細胞内の位置: Host nucleus (By similarity): P03074
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9175.59

構造登録者

Berjanskii, M.V.,Riley, M.I.,Xie, A.,Semenchenko, V.,Folk, W.R.,Van Doren, S.R. (登録日: 2000-07-13, 公開日: 2000-11-22, 最終更新日: 2024-05-22)

主引用文献

Berjanskii, M.V.,Riley, M.I.,Xie, A.,Semenchenko, V.,Folk, W.R.,Van Doren, S.R.
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, 2000

PubMed 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.

PubMed: 10950962
DOI: 10.1074/jbc.M006572200

実験手法

SOLUTION NMR