PDBsum entry 5dis

Transport protein

PDB id: 5dis

Contents

Protein chains

1032 a.a.

172 a.a.

264 a.a.

395 a.a.

Ligands

GLC-GLC

PRO ×2

GTP

Metals

_MG

Waters ×12

PDB id:

5dis

Name:

Transport protein

Title:

Crystal structure of a crm1-rangtp-spn1 export complex bound to a 113 amino acid fg-repeat containing fragment of nup214

Structure:

Exportin-1. Chain: a. Fragment: unp residues 5-1058. Synonym: exp1,chromosome region maintenance 1 protein homolog. Engineered: yes. Gtp-binding nuclear protein ran. Chain: b. Fragment: unp residues 8-179. Synonym: androgen receptor-associated protein 24,gtpase ran,ras-like

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: xpo1, crm1. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: ran, ara24, ok/sw-cl.81. Gene: snupn, rnut1, spn1. Escherichia coli (strain k12), homo sapiens.

Resolution:

2.85Å R-factor: 0.208 R-free: 0.249

Authors:

T.Monecke,S.A.Port,A.Dickmanns,R.H.Kehlenbach,R.Ficner

Key ref:

S.A.Port et al. (2015). Structural and Functional Characterization of CRM1-Nup214 Interactions Reveals Multiple FG-Binding Sites Involved in Nuclear Export. Cell Rep, 13, 690-702. PubMed id: 26489467 DOI: 10.1016/j.celrep.2015.09.042

Date:

01-Sep-15 Release date: 04-Nov-15

Protein chain

O14980  (XPO1_HUMAN) -  Exportin-1 from Homo sapiens

Seq: 1071 a.a.

Struc: 1032 a.a.

Protein chain

P62826  (RAN_HUMAN) -  GTP-binding nuclear protein Ran from Homo sapiens

Seq: 216 a.a.

Struc: 172 a.a.*

Protein chain

O95149  (SPN1_HUMAN) -  Snurportin-1 from Homo sapiens

Seq: 360 a.a.

Struc: 264 a.a.

Protein chain

P0AEX9  (MALE_ECOLI) -  Maltose/maltodextrin-binding periplasmic protein from Escherichia coli (strain K12)

Seq: 396 a.a.

Struc: 395 a.a.*

Protein chain

P35658  (NU214_HUMAN) -  Nuclear pore complex protein Nup214 from Homo sapiens

Seq: 2090 a.a.

Struc: 395 a.a.*

* PDB and UniProt seqs differ at 328 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chain B: E.C.3.6.5.- - ?????

DOI no: 10.1016/j.celrep.2015.09.042

Cell Rep 13:690-702 (2015)

PubMed id: 26489467

Structural and Functional Characterization of CRM1-Nup214 Interactions Reveals Multiple FG-Binding Sites Involved in Nuclear Export.

S.A.Port, T.Monecke, A.Dickmanns, C.Spillner, R.Hofele, H.Urlaub, R.Ficner, R.H.Kehlenbach.

ABSTRACT

CRM1 is the major nuclear export receptor. During translocation through the nuclear pore, transport complexes transiently interact with phenylalanine-glycine (FG) repeats of multiple nucleoporins. On the cytoplasmic side of the nuclear pore, CRM1 tightly interacts with the nucleoporin Nup214. Here, we present the crystal structure of a 117-amino-acid FG-repeat-containing fragment of Nup214, in complex with CRM1, Snurportin 1, and RanGTP at 2.85 Å resolution. The structure reveals eight binding sites for Nup214 FG motifs on CRM1, with intervening stretches that are loosely attached to the transport receptor. Nup214 binds to N- and C-terminal regions of CRM1, thereby clamping CRM1 in a closed conformation and stabilizing the export complex. The role of conserved hydrophobic pockets for the recognition of FG motifs was analyzed in biochemical and cell-based assays. Comparative studies with RanBP3 and Nup62 shed light on specificities of CRM1-nucleoporin binding, which serves as a paradigm for transport receptor-nucleoporin interactions.