PDBsum entry 4pqz

Transcription

PDB id: 4pqz

Contents

Protein chain

136 a.a.

Waters ×25

PDB id:

4pqz

Name:

Transcription

Title:

Crystal structure of swt1 c-terminal domain from yeast

Structure:

Transcriptional protein swt1. Chain: a. Fragment: c-terminal domain (unp residues 312-458). Synonym: synthetically lethal with trex protein 1. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: swt1, yor166c, o3595. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.30Å R-factor: 0.212 R-free: 0.265

Authors:

S.X.Peng,Z.Q.Gao,Q.S.Liu,Y.H.Dong

Key ref:

S.Peng et al. (2014). High-resolution crystal structure reveals a HEPN domain at the C-terminal region of S. cerevisiae RNA endonuclease Swt1. Biochem Biophys Res Commun, 453, 826-832. PubMed id: 25450355 DOI: 10.1016/j.bbrc.2014.10.040

Date:

05-Mar-14 Release date: 03-Dec-14

Protein chain

Q12104  (SWT1_YEAST) -  Transcriptional protein SWT1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 458 a.a.

Struc: 136 a.a.

DOI no: 10.1016/j.bbrc.2014.10.040

Biochem Biophys Res Commun 453:826-832 (2014)

PubMed id: 25450355

High-resolution crystal structure reveals a HEPN domain at the C-terminal region of S. cerevisiae RNA endonuclease Swt1.

S.Peng, K.Zhou, W.Wang, Z.Gao, Y.Dong, Q.Liu.

ABSTRACT

Swt1 is an RNA endonuclease that plays an important role in quality control of nuclear messenger ribonucleoprotein particles (mRNPs) in eukaryotes; however, its structural details remain to be elucidated. Here, we report the crystal structure of the C-terminal (CT) domain of Swt1 from Saccharomyces cerevisiae, which shares common characteristics of higher eukaryotes and prokaryotes nucleotide binding (HEPN) domain superfamily. To study in detail the full-length protein structure, we analyzed the low-resolution architecture of Swt1 in solution using small angle X-ray scattering (SAXS) method. Both the CT domain and middle domain exhibited a good fit upon superimposing onto the molecular envelope of Swt1. Our study provides the necessary structural information for detailed analysis of the functional role of Swt1, and its importance in the process of nuclear mRNP surveillance.