6AF0

Structure of Ctr9, Paf1 and Cdc73 ternary complex from Myceliophthora thermophila

Summary for 6AF0

• Entry DOI: 10.2210/pdb6af0/pdb
• Descriptor: Ctr9 protein, Paf1 protein, Cdc73 protein (3 entities in total)
• Functional Keywords: transcription elongation; paf1; ctr9; cdc73; crystal structure, transcription
• Biological source: Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) (Sporotrichum thermophile); More
• Total number of polymer chains: 3
• Total formula weight: 126894.93

Authors

Wang, Z.,Deng, P.,Zhou, Y. (deposition date: 2018-08-07, release date: 2018-09-19, Last modification date: 2024-03-27)

Primary citation

Deng, P.,Zhou, Y.,Jiang, J.,Li, H.,Tian, W.,Cao, Y.,Qin, Y.,Kim, J.,Roeder, R.G.,Patel, D.J.,Wang, Z.
Transcriptional elongation factor Paf1 core complex adopts a spirally wrapped solenoidal topology.
Proc. Natl. Acad. Sci. U.S.A., 115:9998-10003, 2018

PubMed Abstract: The polymerase-associated factor 1 (Paf1) complex is a general transcription elongation factor of RNA polymerase II, which is composed of five core subunits, Paf1, Ctr9, Cdc73, Leo1, and Rtf1, and functions as a diverse platform that broadly affects gene expression genome-wide. In this study, we solved the 2.9-Å crystal structure of the core region composed of the Ctr9-Paf1-Cdc73 ternary complex from a thermophilic fungi, which provides a structural perspective of the molecular details of the organization and interactions involving the Paf1 subunits in the core complex. We find that Ctr9 is composed of 21 tetratricopeptide repeat (TPR) motifs that wrap three circular turns in a right-handed superhelical manner around the N-terminal region of an elongated single-polypeptide-chain scaffold of Paf1. The Cdc73 fragment is positioned within the surface groove of Ctr9, where it contacts mainly with Ctr9 and minimally with Paf1. We also identified that the Paf1 complex preferentially binds single-strand-containing DNAs. Our work provides structural insights into the overall architecture of the Paf1 complex and paves the road forward for understanding the molecular mechanisms of the Paf1 complex in transcriptional regulation.

PubMed: 30224485
DOI: 10.1073/pnas.1812256115

Experimental method

X-RAY DIFFRACTION (2.88 Å)