PDBsum entry 2ma9

Viral protein/protein binding

PDB id: 2ma9

Contents

Protein chains

32 a.a.

118 a.a.

91 a.a.

PDB id:

2ma9

Name:

Viral protein/protein binding

Title:

HIV-1 vif socs-box and elongin bc solution structure

Structure:

Virion infectivity factor. Chain: a. Fragment: unp residues 139-174. Synonym: vif, sor protein, virion infectivity factor p17, virion infectivity factor p7. Engineered: yes. Transcription elongation factor b polypeptide 2. Chain: b. Synonym: elongin 18 kda subunit, elongin-b, elob, RNA polymerase ii

Source:

Human immunodeficiency virus type 1. HIV-1. Organism_taxid: 11698. Gene: vif. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606.

NMR struc:

20 models

Authors:

Z.Lu,J.R.Bergeron,R.A.Atkinson,T.Schaller,D.A.Veselkov,A.Oregioni, Y.Yang,S.J.Matthews,M.H.Malim,M.R.Sanderson

Key ref:

Z.Lu et al. (2013). Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction. Open Biol, 3, 130100. PubMed id: 24225024 DOI: 10.1098/rsob.130100

Date:

01-Jul-13 Release date: 11-Dec-13

Protein chain

P12504  (VIF_HV1N5) -  Virion infectivity factor from Human immunodeficiency virus type 1 group M subtype B (isolate NY5)

Seq: 192 a.a.

Struc: 32 a.a.

Protein chain

Q15370  (ELOB_HUMAN) -  Elongin-B from Homo sapiens

Seq: 118 a.a.

Struc: 118 a.a.

Protein chain

Q15369  (ELOC_HUMAN) -  Elongin-C from Homo sapiens

Seq: 112 a.a.

Struc: 91 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C: E.C.?

DOI no: 10.1098/rsob.130100

Open Biol 3:130100 (2013)

PubMed id: 24225024

Insight into the HIV-1 Vif SOCS-box-ElonginBC interaction.

Z.Lu, J.R.Bergeron, R.A.Atkinson, T.Schaller, D.A.Veselkov, A.Oregioni, Y.Yang, S.J.Matthews, M.H.Malim, M.R.Sanderson.

ABSTRACT

The HIV-1 viral infectivity factor (Vif) neutralizes cell-encoded antiviral APOBEC3 proteins by recruiting a cellular ElonginB (EloB)/ElonginC (EloC)/Cullin5-containing ubiquitin ligase complex, resulting in APOBEC3 ubiquitination and proteolysis. The suppressors-of-cytokine-signalling-like domain (SOCS-box) of HIV-1 Vif is essential for E3 ligase engagement, and contains a BC box as well as an unusual proline-rich motif. Here, we report the NMR solution structure of the Vif SOCS-ElonginBC (EloBC) complex. In contrast to SOCS-boxes described in other proteins, the HIV-1 Vif SOCS-box contains only one α-helical domain followed by a β-sheet fold. The SOCS-box of Vif binds primarily to EloC by hydrophobic interactions. The functionally essential proline-rich motif mediates a direct but weak interaction with residues 101-104 of EloB, inducing a conformational change from an unstructured state to a structured state. The structure of the complex and biophysical studies provide detailed insight into the function of Vif's proline-rich motif and reveal novel dynamic information on the Vif-EloBC interaction.