PDBsum entry 2k9h

Metal binding protein

PDB id: 2k9h

Contents

Protein chain

57 a.a. *

Metals

_ZN ×2

* Residue conservation analysis

PDB id:

2k9h

Name:

Metal binding protein

Title:

The hantavirus glycoprotein g1 tail contains a dual cchc-type classical zinc fingers

Structure:

Glycoprotein. Chain: a. Engineered: yes

Source:

Andes virus. Organism_taxid: 46607. Strain: andes. Gene: af028026. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

D.F.Estrada,D.M.Boudreaux,D.Zhong,S.C.St Jeor,R.N.De Guzman

Key ref:

D.F.Estrada et al. (2009). The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc Fingers. J Biol Chem, 284, 8654-8660. PubMed id: 19179334 DOI: 10.1074/jbc.M808081200

Date:

13-Oct-08 Release date: 27-Jan-09

Protein chain

Q9E006  (Q9E006_9VIRU) -  Envelopment polyprotein from Andes orthohantavirus

Seq: 1138 a.a.

Struc: 57 a.a.

DOI no: 10.1074/jbc.M808081200

J Biol Chem 284:8654-8660 (2009)

PubMed id: 19179334

The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc Fingers.

D.F.Estrada, D.M.Boudreaux, D.Zhong, S.C.St Jeor, R.N.De Guzman.

ABSTRACT

Hantaviruses are distributed worldwide and can cause a hemorrhagic fever or a cardiopulmonary syndrome in humans. Mature virions consist of RNA genome, nucleocapsid protein, RNA polymerase, and two transmembrane glycoproteins, G1 and G2. The ectodomain of G1 is surface-exposed; however, it has a 142-residue C-terminal cytoplasmic tail that plays important roles in viral assembly and host-pathogen interaction. Here we show by NMR, circular dichroism spectroscopy, and mutagenesis that a highly conserved cysteine/histidine-rich region in the G1 tail of hantaviruses forms two CCHC-type classical zinc fingers. Unlike classical zinc fingers, however, the two G1 zinc fingers are intimately joined together, forming a compact domain with a unique fold. We discuss the implication of the hantaviral G1 zinc fingers in viral assembly and host-pathogen interaction.

Selected figure(s)

Figure 1.
The G1 tail of Hantaviruses, Nairoviruses, and Orthobunyaviruses (genera of Bunyaviridae) contains a cysteine/histidine-rich region with two CCHC arrays. Structure determination of the Andes virus dual CCHC-region revealed a novel zinc finger domain. Shown are the secondary structures (α-helices and β-strands), zinc-coordinating residues (blocked), the two CCHC motifs (boxed), conserved residues (gray), and residue numbers for the Andes virus G1 sequence. Sequence alignment was generated using CLUSTALW and formatted with ESPript 2.2 (53).

Figure 4.
The NMR structure of the Andes virus G1 tail zinc-binding domain reveals two classical ββα fold zinc fingers that are joined together. A, stereoview of the superposition of 20 lowest energy NMR structures. B and C, ribbon structures of the lowest energy NMR structure showing the residues involved in the first (ZF1) (B) and second (ZF2) (C) zinc fingers. Shown are the cysteine and histidine residues (yellow) that coordinate Zn^2+ ions (gray) as well as the secondary structures (α[1]-α[2], β[1]-β[2]). The dual hantaviral G1 zinc fingers interact with each other and form a single domain with a novel fold as revealed by DALI (40) and TM-align (41) structural homology searches.

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2009, 284, 8654-8660) copyright 2009.

Figures were selected by an automated process.