2YN2

Huf protein - paralogue of the tau55 histidine phosphatase domain

Summary for 2YN2

• Entry DOI: 10.2210/pdb2yn2/pdb
• Descriptor: UNCHARACTERIZED PROTEIN YNL108C, FORMIC ACID (3 entities in total)
• Functional Keywords: hydrolase, histidine phosphatase domain, phosphoglycerate mutase domain
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 1
• Total formula weight: 32019.47

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: 2023-12-20)

Primary citation

Taylor, N.M.I.,Glatt, S.,Hennrich, M.L.,Von Scheven, G.,Grotsch, H.,Fernandez-Tornero, C.,Rybin, V.,Gavin, A.,Kolb, P.,Muller, C.W.
Structural and Functional Characterization of a Phosphatase Domain within Yeast General Transcription Factor Tfiiic.
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 (2.05 Å)