PDBsum entry 5b56

Protein transport/viral protein

PDB id: 5b56

Contents

Protein chains

429 a.a.

12 a.a.

Waters ×512

PDB id:

5b56

Name:

Protein transport/viral protein

Title:

Crystal structure of HIV-1 vpr c-terminal domain and dibb-m-importin- alpha2 complex

Structure:

Importin subunit alpha-1. Chain: a, b. Fragment: unp residues 70-529. Synonym: importin alpha p1,karyopherin subunit alpha-2,pendulin,pore targeting complex 58 kda subunit,ptac58,rag cohort protein 1,srp1- alpha. Engineered: yes. Protein vpr. Chain: c, d, e, f.

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: kpna2. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. HIV-1 m:b_89.6. HIV-1.

Resolution:

2.30Å R-factor: 0.184 R-free: 0.226

Authors:

H.Miyatake,A.Sanjoh,G.Matusda,T.Murakami,H.Murakami,K.Hagiwara, M.Yokoyama,H.Sato,Y.Miyamoto,N.Dohmae,Y.Aida

Key ref:

H.Miyatake et al. (2016). Molecular Mechanism of HIV-1 Vpr for Binding to Importin-α. J Mol Biol, 428, 2744-2757. PubMed id: 27181198 DOI: 10.1016/j.jmb.2016.05.003

Date:

25-Apr-16 Release date: 01-Jun-16

Protein chains

P52293  (IMA1_MOUSE) -  Importin subunit alpha-1 from Mus musculus

Seq: 529 a.a.

Struc: 429 a.a.

Protein chains

Q73369  (VPR_HV1B9) -  Protein Vpr from Human immunodeficiency virus type 1 group M subtype B (strain 89.6)

Seq: 96 a.a.

Struc: 12 a.a.

DOI no: 10.1016/j.jmb.2016.05.003

J Mol Biol 428:2744-2757 (2016)

PubMed id: 27181198

Molecular Mechanism of HIV-1 Vpr for Binding to Importin-α.

H.Miyatake, A.Sanjoh, T.Murakami, H.Murakami, G.Matsuda, K.Hagiwara, M.Yokoyama, H.Sato, Y.Miyamoto, N.Dohmae, Y.Aida.

ABSTRACT

Viral protein R (Vpr) is an accessory gene product of human immunodeficiency virus type 1 (HIV-1) that plays multiple important roles associated with viral replication. Structural studies using NMR have revealed that Vpr consists of three α-helices and contains flexible N- and C-termini. However, the molecular mechanisms associated with Vpr function have not been elucidated. To investigate Vpr multifunctionality, we performed an X-ray crystallographic study of Vpr complexes containing importin-α, a known Vpr binding partner present in host cells. Elucidation of the crystal structure revealed that the flexible C-terminus changes its conformation to a twisted β-turn via an induced-fit mechanism, enabling binding to a minor nuclear localization signal (NLS) site of importin-α. The Vpr C-terminus can also bind with major NLS sites of importin-α in an extended conformation in different ways. These results, which represent the first reported crystallographic analysis of Vpr, demonstrate the multifunctional aspects that enable Vpr interaction with a variety of cellular proteins.