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PDBsum entry 3zd7
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Hydrolase/RNA
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PDB id
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3zd7
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PDB id:
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| Name: |
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Hydrolase/RNA
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Title:
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Snapshot 3 of rig-i scanning on RNA duplex
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Structure:
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Probable atp-dependent RNA helicase ddx58. Chain: a. 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. RNA duplex. Chain: c, d. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Synthetic: yes. Synthetic construct. Organism_taxid: 32630
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Resolution:
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2.50Å
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R-factor:
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0.232
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R-free:
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0.288
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Authors:
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D.Luo,A.M.Pyle
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Key ref:
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A.Kohlway
et al.
(2013).
Defining the functional determinants for RNA surveillance by RIG-I.
Embo Rep,
14,
772-779.
PubMed id:
DOI:
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Date:
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25-Nov-12
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Release date:
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07-Aug-13
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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.
623 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 4 residue positions (black
crosses)
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G-C-G-C-G-C-G-C-G-C
10 bases
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G-C-G-C-G-C-G-C-G-C
10 bases
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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
Bound ligand (Het Group name = )
corresponds exactly
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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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Embo Rep
14:772-779
(2013)
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PubMed id:
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Defining the functional determinants for RNA surveillance by RIG-I.
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A.Kohlway,
D.Luo,
D.C.Rawling,
S.C.Ding,
A.M.Pyle.
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ABSTRACT
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Retinoic acid-inducible gene-I (RIG-I) is an intracellular RNA sensor that
activates the innate immune machinery in response to infection by RNA viruses.
Here, we report the crystal structure of distinct conformations of a RIG-I:dsRNA
complex, which shows that HEL2i-mediated scanning allows RIG-I to sense the
length of RNA targets. To understand the implications of HEL2i scanning for
catalytic activity and signalling by RIG-I, we examined its ATPase activity when
stimulated by duplex RNAs of varying lengths and 5' composition. We identified a
minimal RNA duplex that binds one RIG-I molecule, stimulates robust ATPase
activity, and elicits a RIG-I-mediated interferon response in cells. Our results
reveal that the minimal functional unit of the RIG-I:RNA complex is a monomer
that binds at the terminus of a duplex RNA substrate. This behaviour is markedly
different from the RIG-I paralog melanoma differentiation-associated gene 5
(MDA5), which forms cooperative filaments.
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Links
