PDBsum entry 6b4j

Transport protein

PDB id: 6b4j

Contents

Protein chains

315 a.a.

44 a.a.

38 a.a.

426 a.a.

Ligands

PO4 ×6

ANP ×2

Metals

_MG ×2

PDB id:

6b4j

Name:

Transport protein

Title:

Crystal structure of human gle1 ctd-nup42 gbm-ddx19b(amppnp) complex

Structure:

Nucleoporin gle1. Chain: b, a. Synonym: hgle1,gle1-like protein. Engineered: yes. Nucleoporin like 2. Chain: c, d. Engineered: yes. Atp-dependent RNA helicase ddx19b. Chain: e, f.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: gle1, gle1l. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: nupl2. Gene: ddx19b, dbp5, ddx19, tdbp. Expression_system_taxid: 562

Resolution:

3.40Å R-factor: 0.266 R-free: 0.313

Authors:

D.H.Lin,A.R.Correia,S.W.Cai,F.M.Huber,C.A.Jette,A.Hoelz

Key ref:

D.H.Lin et al. (2018). Structural and functional analysis of mRNA export regulation by the nuclear pore complex. Nat Commun, 9, 2319. PubMed id: 29899397

Date:

26-Sep-17 Release date: 20-Jun-18

Protein chains

Q53GS7  (GLE1_HUMAN) -  mRNA export factor GLE1 from Homo sapiens

Seq: 698 a.a.

Struc: 315 a.a.

Protein chain

O15504  (NUP42_HUMAN) -  Nucleoporin NUP42 from Homo sapiens

Seq: 423 a.a.

Struc: 44 a.a.

Protein chain

O15504  (NUP42_HUMAN) -  Nucleoporin NUP42 from Homo sapiens

Seq: 423 a.a.

Struc: 38 a.a.

Protein chains

Q9UMR2  (DD19B_HUMAN) -  ATP-dependent RNA helicase DDX19B from Homo sapiens

Seq: 479 a.a.

Struc: 426 a.a.

Enzyme reactions

• Enzyme class: Chains E, F: E.C.3.6.4.13 - Rna helicase.
• Reaction: ATP + H2O = ADP + phosphate + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

Nat Commun 9:2319 (2018)

PubMed id: 29899397

Structural and functional analysis of mRNA export regulation by the nuclear pore complex.

D.H.Lin, A.R.Correia, S.W.Cai, F.M.Huber, C.A.Jette, A.Hoelz.

ABSTRACT

The nuclear pore complex (NPC) controls the passage of macromolecules between the nucleus and cytoplasm, but how the NPC directly participates in macromolecular transport remains poorly understood. In the final step of mRNA export, the DEAD-box helicase DDX19 is activated by the nucleoporins Gle1, Nup214, and Nup42 to remove Nxf1•Nxt1 from mRNAs. Here, we report crystal structures of Gle1•Nup42 from three organisms that reveal an evolutionarily conserved binding mode. Biochemical reconstitution of the DDX19 ATPase cycle establishes that human DDX19 activation does not require IP₆, unlike its fungal homologs, and that Gle1 stability affects DDX19 activation. Mutations linked to motor neuron diseases cause decreased Gle1 thermostability, implicating nucleoporin misfolding as a disease determinant. Crystal structures of human Gle1•Nup42•DDX19 reveal the structural rearrangements in DDX19 from an auto-inhibited to an RNA-binding competent state. Together, our results provide the foundation for further mechanistic analyses of mRNA export in humans.