2YN0

tau55 histidine phosphatase domain

Summary for 2YN0

• Entry DOI: 10.2210/pdb2yn0/pdb
• Descriptor: TRANSCRIPTION FACTOR TAU 55 KDA SUBUNIT, PHOSPHATE ION (3 entities in total)
• Functional Keywords: transcription, rna polymerase iii
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 1
• Total formula weight: 31142.00

Authors

Taylor, N.M.I.,Glatt, S.,Hennrich, M.,von Scheven, G.,Grotsch, H.,Fernandez-Tornero, C.,Rybin, V.,Gavin, A.C.,Kolb, P.,Muller, C.W. (deposition date: 2012-10-11, release date: 2013-04-03, Last modification date: 2024-05-08)

Primary citation

Taylor, N.M.I.,Glatt, S.,Hennrich, M.L.,Von Scheven, G.,Grotsch, H.,Fernandez-Tornero, C.,Rybin, V.,Gavin, A.C.,Kolb, P.,Muller, C.W.
Structural and Functional Characterization of a Phosphatase Domain within Yeast General Transcription Factor Iiic.
J.Biol.Chem., 288:15110-, 2013

PubMed Abstract: Saccharomyces cerevisiae τ55, a subunit of the RNA polymerase III-specific general transcription factor TFIIIC, comprises an N-terminal histidine phosphatase domain (τ55-HPD) whose catalytic activity and cellular function is poorly understood. We solved the crystal structures of τ55-HPD and its closely related paralogue Huf and used in silico docking methods to identify phosphoserine- and phosphotyrosine-containing peptides as possible substrates that were subsequently validated using in vitro phosphatase assays. A comparative phosphoproteomic study identified additional phosphopeptides as possible targets that show the involvement of these two phosphatases in the regulation of a variety of cellular functions. Our results identify τ55-HPD and Huf as bona fide protein phosphatases, characterize their substrate specificities, and provide a small set of regulated phosphosite targets in vivo.

PubMed: 23569204
DOI: 10.1074/JBC.M112.427856

Experimental method

X-RAY DIFFRACTION (1.5 Å)