PDBsum entry 4wpm

Transport protein

PDB id: 4wpm

Contents

Protein chains

85 a.a.

Ligands

SO4 ×3

Waters ×53

PDB id:

4wpm

Name:

Transport protein

Title:

Structure of the chaetomium thermophilum mex67:mtr2 complex

Structure:

mRNA export protein. Chain: a, b. Fragment: rrm domain, unp residues 93-200. Engineered: yes

Source:

Chaetomium thermophilum. Organism_taxid: 759272. Strain: dsm 1495 / cbs 144.50 / imi 039719. Gene: ctht_0059630. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.40Å R-factor: 0.229 R-free: 0.246

Authors:

S.Aibara,E.Valkov,M.Stewart

Key ref:

S.Aibara et al. (2015). Structural characterization of the principal mRNA-export factor Mex67-Mtr2 from Chaetomium thermophilum. Acta Crystallogr F Struct Biol Commun, 71, 876-888. PubMed id: 26144233 DOI: 10.1107/S2053230X15008766

Date:

20-Oct-14 Release date: 15-Jul-15

Protein chains

G0SET4  (G0SET4_CHATD) -  Putative mRNA export protein from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

Seq: 657 a.a.

Struc: 85 a.a.

DOI no: 10.1107/S2053230X15008766

Acta Crystallogr F Struct Biol Commun 71:876-888 (2015)

PubMed id: 26144233

Structural characterization of the principal mRNA-export factor Mex67-Mtr2 from Chaetomium thermophilum.

S.Aibara, E.Valkov, M.H.Lamers, L.Dimitrova, E.Hurt, M.Stewart.

ABSTRACT

Members of the Mex67-Mtr2/NXF-NXT1 family are the principal mediators of the nuclear export of mRNA. Mex67/NXF1 has a modular structure based on four domains (RRM, LRR, NTF2-like and UBA) that are thought to be present across species, although the level of sequence conservation between organisms, especially in lower eukaryotes, is low. Here, the crystal structures of these domains from the thermophilic fungus Chaetomium thermophilum are presented together with small-angle X-ray scattering (SAXS) and in vitro RNA-binding data that indicate that, not withstanding the limited sequence conservation between different NXF family members, the molecules retain similar structural and RNA-binding properties. Moreover, the resolution of crystal structures obtained with the C. thermophilum domains was often higher than that obtained previously and, when combined with solution and biochemical studies, provided insight into the structural organization, self-association and RNA-binding properties of Mex67-Mtr2 that facilitate mRNA nuclear export.