2YN2: Huf protein - paralogue of the tau55 histidine phosphatase domain

Citation:
Abstract
Saccharomyces cerevisiae tau55, a subunit of the RNA polymerase III-specific general transcription factor TFIIIC, comprises an N-terminal histidine phosphatase domain (tau55-HPD) whose catalytic activity and cellular function is poorly understood. We solved the crystal structures of tau55-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 tau55-HPD and Huf as bona fide protein phosphatases, characterize their substrate specificities, and provide a small set of regulated phosphosite targets in vivo.
PDB ID: 2YN2Download
MMDB ID: 108759
PDB Deposition Date: 2012/10/11
Updated in MMDB: 2018/07
Experimental Method:
x-ray diffraction
Resolution: 2.05  Å
Source Organism:
Similar Structures:
Biological Unit for 2YN2: monomeric; determined by author and by software (PISA)
Molecular Components in 2YN2
Label Count Molecule
Protein (1 molecule)
1
Uncharacterized Protein Ynl108c(Gene symbol: YNL108C)
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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