PDBsum entry 4m6t

Transcription regulator

PDB id: 4m6t

Contents

Protein chain

177 a.a.

Ligands

SAM

Waters ×4

PDB id:

4m6t

Name:

Transcription regulator

Title:

Structure of human paf1 and leo1 complex

Structure:

RNA polymerase ii-associated factor 1 homolog, linker, RNA polymerase-associated protein leo1. Chain: a. Fragment: unp residues 170-250 of paf1, unp residues 370-462 of leo1. Engineered: yes. Other_details: chimera of RNA polymerase ii-associated factor 1 homolog, linker, RNA polymerase-associated protein leo1

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: paf1, leo1. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.50Å R-factor: 0.234 R-free: 0.268

Authors:

Y.Shen,X.Qin

Key ref:

X.Chu et al. (2013). Structural insights into Paf1 complex assembly and histone binding. Nucleic Acids Res, 41, 10619-10629. PubMed id: 24038468 DOI: 10.1093/nar/gkt819

Date:

11-Aug-13 Release date: 02-Oct-13

Protein chain

Q8N7H5  (PAF1_HUMAN) -  RNA polymerase II-associated factor 1 homolog from Homo sapiens

Seq: 531 a.a.

Struc: 177 a.a.*

Protein chain

Q8WVC0  (LEO1_HUMAN) -  RNA polymerase-associated protein LEO1 from Homo sapiens

Seq: 666 a.a.

Struc: 177 a.a.*

* PDB and UniProt seqs differ at 161 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1093/nar/gkt819

Nucleic Acids Res 41:10619-10629 (2013)

PubMed id: 24038468

Structural insights into Paf1 complex assembly and histone binding.

X.Chu, X.Qin, H.Xu, L.Li, Z.Wang, F.Li, X.Xie, H.Zhou, Y.Shen, J.Long.

ABSTRACT

The highly conserved Paf1 complex (PAF1C) plays critical roles in RNA polymerase II transcription elongation and in the regulation of histone modifications. It has also been implicated in other diverse cellular activities, including posttranscriptional events, embryonic development and cell survival and maintenance of embryonic stem cell identity. Here, we report the structure of the human Paf1/Leo1 subcomplex within PAF1C. The overall structure reveals that the Paf1 and Leo1 subunits form a tightly associated heterodimer through antiparallel beta-sheet interactions. Detailed biochemical experiments indicate that Leo1 binds to PAF1C through Paf1 and that the Ctr9 subunit is the key scaffold protein in assembling PAF1C. Furthermore, we show that the Paf1/Leo1 heterodimer is necessary for its binding to histone H3, the histone octamer, and nucleosome in vitro. Our results shed light on the PAF1C assembly process and substrate recognition during various PAF1C-coordinated histone modifications.