5X4Z

RNA Polymerase II from Komagataella Pastoris (Type-1 crystal)

Summary for 5X4Z

• Entry DOI: 10.2210/pdb5x4z/pdb
• Related: 5X50 5X51
• Descriptor: DNA-directed RNA polymerase subunit, RNA polymerase subunit ABC10-beta, common to RNA polymerases I, II, and III, RNA polymerase II subunit B12.5, ... (13 entities in total)
• Functional Keywords: transcription, rna polymerase, transferase
• Biological source: Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast); More
• Cellular location: Nucleus, nucleolus : F2QPE6
• Total number of polymer chains: 24
• Total formula weight: 1022011.31

Authors

Ehara, H.,Umehara, T.,Sekine, S.,Yokoyama, S. (deposition date: 2017-02-14, release date: 2017-05-17, Last modification date: 2024-10-16)

Primary citation

Ehara, H.,Umehara, T.,Sekine, S.I.,Yokoyama, S.
Crystal structure of RNA polymerase II from Komagataella pastoris
Biochem. Biophys. Res. Commun., 487:230-235, 2017

PubMed Abstract: RNA polymerase II (Pol II) is a 12-subunit protein complex that conducts the transcription of mRNA and some small RNAs. In this work, the crystal structure of Pol II from the methylotropic yeast Komagataella pastoris (Pichia pastoris) was determined. While the structure is highly homologous to that of Pol II from the budding yeast Saccharomyces cerevisiae, the stalk and clamp modules of the K. pastoris Pol II displayed large inward rotations, closing the central cleft to a greater extent than in the known S. cerevisiae Pol II structures. The conformational differences reflect the inherent flexibilities of the stalk and the clamp, as additional low-resolution structures of K. pastoris Pol II in different crystal forms revealed diverse stalk and clamp orientations. Comparisons with other eukaryotic/archaeal RNA polymerase structures in the Protein Data Bank revealed the distributions of the stalk and clamp orientations. The conformational plasticity should be essential for transcriptional functions and binding various regulatory factors.

PubMed: 28412353
DOI: 10.1016/j.bbrc.2017.04.039

Experimental method

X-RAY DIFFRACTION (7.8 Å)