2YN0

tau55 histidine phosphatase domain

PDB DOI: https://doi.org/10.2210/pdb2YN0/pdb

Classification: TRANSCRIPTION
Organism(s): Saccharomyces cerevisiae S288C
Expression System: Trichoplusia ni
Mutation(s): No

Deposited: 2012-10-11 Released: 2013-04-03
Deposition Author(s): 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.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.50 Å
R-Value Free: 0.183
R-Value Work: 0.156
R-Value Observed: 0.157

wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

Structural and Functional Characterization of a Phosphatase Domain within Yeast General Transcription Factor Iiic.

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.

(2013) J Biol Chem 288: 15110

PubMed: 23569204 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1074/jbc.M112.427856
Primary Citation of Related Structures:
2YN0, 2YN2

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.

Organizational Affiliation

Structural and Computational Biology Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.

Macromolecule Content

Total Structure Weight: 31.14 kDa
Atom Count: 2,381
Modelled Residue Count: 248
Deposited Residue Count: 271
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
TRANSCRIPTION FACTOR TAU 55 KDA SUBUNIT	A	271	Saccharomyces cerevisiae S288C	Mutation(s): 0
UniProt
Find proteins for Q12415 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore Q12415 Go to UniProtKB: Q12415
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q12415
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
PO4 Query on PO4 Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A]	B [auth A]	PHOSPHATE ION O₄ P NBIIXXVUZAFLBC-UHFFFAOYSA-K		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.50 Å
R-Value Free: 0.183
R-Value Work: 0.156
R-Value Observed: 0.157
Space Group: P 2₁ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 80.58	α = 90
b = 86.73	β = 90
c = 44.31	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
XDS	data reduction
XSCALE	data scaling
SHARP	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2013-04-03

Deposition Author(s):

Fernandez-Tornero, C.

Revision History (Full details and data files)

Version 1.0: 2013-04-03
Type: Initial release
Version 1.1: 2013-04-17
Changes: Database references
Version 1.2: 2013-06-12
Changes: Database references
Version 1.3: 2019-04-03
Changes: Data collection, Other, Source and taxonomy