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PDBsum entry 4on9
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PDB id:
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Hydrolase
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Title:
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Dech box helicase domain
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Structure:
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Probable atp-dependent RNA helicase ddx58. Chain: a, b. Fragment: unp residues 230-793. Synonym: dead box protein 58, rig-i-like receptor 1, rlr-1, retinoic acid-inducible gene 1 protein, rig-1, retinoic acid-inducible gene i protein, rig-i. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: ddx58. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.71Å
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R-factor:
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0.221
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R-free:
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0.258
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Authors:
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T.Deimling,G.Witte,K.P.Hopfner
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Key ref:
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T.Deimling
et al.
(2014).
Crystal and solution structure of the human RIG-I SF2 domain.
Acta Crystallogr F Struct Biol Commun,
70,
1027-1031.
PubMed id:
DOI:
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Date:
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28-Jan-14
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Release date:
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02-Jul-14
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PROCHECK
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Headers
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References
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O95786
(DDX58_HUMAN) -
Antiviral innate immune response receptor RIG-I from Homo sapiens
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Seq:
Struc:
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925 a.a.
514 a.a.
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Key: |
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Secondary structure |
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CATH domain |
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Enzyme class:
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E.C.3.6.4.13
- Rna helicase.
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Reaction:
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ATP + H2O = ADP + phosphate + H+
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ATP
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+
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H2O
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=
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ADP
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+
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phosphate
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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Acta Crystallogr F Struct Biol Commun
70:1027-1031
(2014)
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PubMed id:
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Crystal and solution structure of the human RIG-I SF2 domain.
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T.Deimling,
S.Cui,
K.Lammens,
K.P.Hopfner,
G.Witte.
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ABSTRACT
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RIG-I is a pathogen-recognition receptor that recognizes viral 5'-triphosphates
carrying double-stranded RNA. Upon binding to these microbe-associated molecular
patterns (MAMPs), RIG-I forms oligomers and promotes downstream processes that
result in type I interferon production and induction of an antiviral state.
Here, the crystal structure of the human RIG-I superfamily 2 ATPase domain
crystallized in an unusually elongated and open conformation is reported. The
elongated structure is probably induced in part by crystal packing, but
nevertheless indicates that the domain is intrinsically very flexible. This
flexibility might allow substantial structural changes upon substrate binding
and oligomerization.
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