1faf
From Proteopedia
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NMR STRUCTURE OF THE N-TERMINAL J DOMAIN OF MURINE POLYOMAVIRUS T ANTIGENS.
Overview
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.
About this Structure
1FAF is a Single protein structure of sequence from Murine polyomavirus. Full crystallographic information is available from OCA.
Reference
NMR structure of the N-terminal J domain of murine polyomavirus T antigens. Implications for DnaJ-like domains and for mutations of T antigens., Berjanskii MV, Riley MI, Xie A, Semenchenko V, Folk WR, Van Doren SR, J Biol Chem. 2000 Nov 17;275(46):36094-103. PMID:10950962
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