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PDBsum entry 2k9h
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Metal binding protein
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PDB id
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2k9h
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References listed in PDB file
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Key reference
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Title
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The hantavirus glycoprotein g1 tail contains dual cchc-Type classical zinc fingers.
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Authors
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D.F.Estrada,
D.M.Boudreaux,
D.Zhong,
S.C.St jeor,
R.N.De guzman.
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Ref.
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J Biol Chem, 2009,
284,
8654-8660.
[DOI no: ]
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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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.
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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).
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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.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2009,
284,
8654-8660)
copyright 2009.
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