1w1n
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(New page: 200px<br /><applet load="1w1n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w1n" /> '''THE SOLUTION STRUCTURE OF THE FATC DOMAIN OF...)
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Revision as of 03:04, 21 November 2007
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THE SOLUTION STRUCTURE OF THE FATC DOMAIN OF THE PROTEIN KINASE TOR1 FROM YEAST
Overview
The target of rapamycin (TOR) is a highly conserved Ser/Thr kinase that, plays a central role in the control of cellular growth. TOR has a, characteristic multidomain structure. Only the kinase domain has catalytic, function; the other domains are assumed to mediate interactions with TOR, substrates and regulators. Except for the rapamycin-binding domain, there, are no high-resolution structural data available for TOR. Here, we present, a structural, biophysical, and mutagenesis study of the extremely, conserved COOH-terminal FATC domain. The importance of this domain for TOR, function has been highlighted in several publications. We show that the, FATC domain, in its oxidized form, exhibits a novel structural motif, consisting of an alpha-helix and a COOH-terminal disulfide-bonded loop, between two completely conserved cysteine residues. Upon reduction, the, flexibility of the loop region increases dramatically. The structural, data, the redox potential of the disulfide bridge, and the biochemical, data of a cysteine to serine mutant indicate that the intracellular redox, potential can affect the cellular amount of the TOR protein via the FATC, domain. Because the amount of TOR mRNA is not changed, the redox state of, the FATC disulfide bond is probably influencing the degradation of TOR.
About this Structure
1W1N is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as Phosphatidylinositol 3-kinase, with EC number 2.7.1.137 Full crystallographic information is available from OCA.
Reference
The solution structure of the FATC domain of the protein kinase target of rapamycin suggests a role for redox-dependent structural and cellular stability., Dames SA, Mulet JM, Rathgeb-Szabo K, Hall MN, Grzesiek S, J Biol Chem. 2005 May 27;280(21):20558-64. Epub 2005 Mar 16. PMID:15772072
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