3EF1

The Structure of Fcp1, an essential RNA polymerase II CTD phosphatase

Summary for 3EF1

• Entry DOI: 10.2210/pdb3ef1/pdb
• Related: 3EF0
• Descriptor: RNA polymerase II subunit A C-terminal domain phosphatase, MAGNESIUM ION (3 entities in total)
• Functional Keywords: phosphatase, ctd, fcph, brct, hydrolase, bef3, acylphosphate analog, cobalt, magnesium, manganese, metal-binding, nucleus, protein phosphatase
• Biological source: Schizosaccharomyces pombe (Fission yeast)
• Cellular location: Nucleus : Q9P376
• Total number of polymer chains: 1
• Total formula weight: 50384.11

Authors

Ghosh, A.,Lima, C.D. (deposition date: 2008-09-07, release date: 2008-12-02, Last modification date: 2024-10-16)

Primary citation

Ghosh, A.,Shuman, S.,Lima, C.D.
The structure of Fcp1, an essential RNA polymerase II CTD phosphatase.
Mol.Cell, 32:478-490, 2008

PubMed Abstract: Kinases and phosphatases regulate mRNA synthesis and processing by phosphorylating and dephosphorylating the C-terminal domain (CTD) of the largest subunit of RNA polymerase II. Fcp1 is an essential CTD phosphatase that preferentially hydrolyzes Ser2-PO(4) of the tandem YSPTSPS CTD heptad array. Fcp1 crystal structures were captured at two stages of the reaction pathway: a Mg-BeF(3) complex that mimics the aspartylphosphate intermediate and a Mg-AlF(4)(-) complex that mimics the transition state of the hydrolysis step. Fcp1 is a Y-shaped protein composed of an acylphosphatase domain located at the base of a deep canyon formed by flanking modules that are missing from the small CTD phosphatase (SCP) clade: an Fcp1-specific helical domain and a C-terminal BRCA1 C-terminal (BRCT) domain. The structure and mutational analysis reveals that Fcp1 and Scp1 (a Ser5-selective phosphatase) adopt different CTD-binding modes; we surmise the CTD threads through the Fcp1 canyon to access the active site.

PubMed: 19026779
DOI: 10.1016/j.molcel.2008.09.021

Experimental method

X-RAY DIFFRACTION (2.15 Å)