PDBsum entry 4l1u

Transcription/peptide

PDB id: 4l1u

Contents

Protein chains

130 a.a.

134 a.a.

11 a.a.

Ligands

GLY-SER-ARG-TPO-PRO-MET-TYR-GLY

ARG-TPO-PRO-MET-TYR

SER-ARG-TPO-PRO-MET

SO4 ×29

GOL ×4

Waters ×105

PDB id:

4l1u

Name:

Transcription/peptide

Title:

Crystal structure of human rtf1 plus3 domain in complex with spt5 ctr phosphopeptide

Structure:

RNA polymerase-associated protein rtf1 homolog. Chain: a, b, c, d, e, f. Fragment: plus3, unp residues 353-484. Engineered: yes. Transcription elongation factor spt5. Chain: g, h, i, j. Fragment: ctr, unp residues 778-790. Synonym: hspt5, drb sensitivity-inducing factor 160 kda subunit, dsif p160, drb sensitivity-inducing factor large subunit, dsif large

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: kiaa0252, rtf1. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Other_details: this sequence occurs naturally in human spt5

Resolution:

2.42Å R-factor: 0.180 R-free: 0.226

Authors:

A.D.Wier,A.Heroux,A.P.Vandemark

Key ref:

A.D.Wier et al. (2013). Structural basis for Spt5-mediated recruitment of the Paf1 complex to chromatin. Proc Natl Acad Sci U S A, 110, 17290-17295. PubMed id: 24101474 DOI: 10.1073/pnas.1314754110

Date:

03-Jun-13 Release date: 02-Oct-13

Protein chain

Q92541  (RTF1_HUMAN) -  RNA polymerase-associated protein RTF1 homolog from Homo sapiens

Seq: 710 a.a.

Struc: 130 a.a.*

Protein chains

Q92541  (RTF1_HUMAN) -  RNA polymerase-associated protein RTF1 homolog from Homo sapiens

Seq: 710 a.a.

Struc: 134 a.a.*

Protein chain

O00267  (SPT5H_HUMAN) -  Transcription elongation factor SPT5 from Homo sapiens

Seq: 1087 a.a.

Struc: 11 a.a.*

* PDB and UniProt seqs differ at 8 residue positions (black crosses)

DOI no: 10.1073/pnas.1314754110

Proc Natl Acad Sci U S A 110:17290-17295 (2013)

PubMed id: 24101474

Structural basis for Spt5-mediated recruitment of the Paf1 complex to chromatin.

A.D.Wier, M.K.Mayekar, A.Héroux, K.M.Arndt, A.P.VanDemark.

ABSTRACT

Polymerase associated factor 1 complex (Paf1C) broadly influences gene expression by regulating chromatin structure and the recruitment of RNA-processing factors during transcription elongation. The Plus3 domain of the Rtf1 subunit mediates Paf1C recruitment to genes by binding a repeating domain within the elongation factor Spt5 (suppressor of Ty). Here we provide a molecular description of this interaction by reporting the structure of human Rtf1 Plus3 in complex with a phosphorylated Spt5 repeat. We find that Spt5 binding is mediated by an extended surface containing phosphothreonine recognition and hydrophobic interfaces that interact with residues outside the Spt5 motif. Changes within these interfaces diminish binding of Spt5 in vitro and chromatin localization of Rtf1 in vivo. The structure reveals the basis for recognition of the repeat motif of Spt5, a key player in the recruitment of gene regulatory factors to RNA polymerase II.