1TA0

Three-dimensional structure of a RNA-polymerase II binding protein with associated ligand.

Summary for 1TA0

• Entry DOI: 10.2210/pdb1ta0/pdb
• Related: 1T9Z
• Descriptor: Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1, MAGNESIUM ION, CITRIC ACID, ... (4 entities in total)
• Functional Keywords: alpha-beta protein, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9GZU7
• Total number of polymer chains: 1
• Total formula weight: 22932.16

Authors

Kamenski, T.,Heilmeier, S.,Meinhart, T.,Cramer, P. (deposition date: 2004-05-19, release date: 2004-08-31, Last modification date: 2024-10-16)

Primary citation

Kamenski, T.,Heilmeier, S.,Meinhart, T.,Cramer, P.
Structure and Mechanism of RNA Polymerase II CTD Phosphatases.
Mol.Cell, 15:399-407, 2004

PubMed Abstract: Recycling of RNA polymerase II (Pol II) after transcription requires dephosphorylation of the polymerase C-terminal domain (CTD) by the phosphatase Fcp1. We report the X-ray structure of the small CTD phosphatase Scp1, which is homologous to the Fcp1 catalytic domain. The structure shows a core fold and an active center similar to those of phosphotransferases and phosphohydrolases that solely share a DXDX(V/T) signature motif with Fcp1/Scp1. We demonstrate that the first aspartate in the signature motif undergoes metal-assisted phosphorylation during catalysis, resulting in a phosphoaspartate intermediate that was structurally mimicked with the inhibitor beryllofluoride. Specificity may result from CTD binding to a conserved hydrophobic pocket between the active site and an insertion domain that is unique to Fcp1/Scp1. Fcp1 specificity may additionally arise from phosphatase recruitment near the CTD via the Pol II subcomplex Rpb4/7, which is shown to be required for binding of Fcp1 to the polymerase in vitro.

PubMed: 15304220
DOI: 10.1016/j.molcel.2004.06.035

Experimental method

X-RAY DIFFRACTION (2.1 Å)