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Literature summary for 4.6.1.19 extracted from

  • Huang, H.; Zeqiraj, E.; Dong, B.; Jha, B.K.; Duffy, N.M.; Orlicky, S.; Thevakumaran, N.; Talukdar, M.; Pillon, M.C.; Ceccarelli, D.F.; Wan, L.C.; Juang, Y.C.; Mao, D.Y.; Gaughan, C.; Brinton, M.A.; Perelygin, A.A.; Kourinov, I.; Guarne, A.; Silverman, R.H.; Sicheri, F.
    Dimeric structure of pseudokinase RNase L bound to 2-5A reveals a basis for interferon-induced antiviral activity (2014), Mol. Cell, 53, 221-234.
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
2',5'-Oligoadenylate the enzyme's pseudokinase domain is involved in the natural activator sensing, binding site and structure, modeling, overview. Quantitative determination of specific binding of the full-length enzyme and of isolated enzyme ANK domain to immobilized biotinylated 2',5'-oligoadenylate Homo sapiens
2',5'-Oligoadenylate the enzyme's pseudokinase domain is involved in the natural activator sensing, binding site and structure, modeling, overview. Quantitative determination of specific binding of the full-length enzyme and of isolated enzyme ANK domain to immobilized biotinylated 2',5'-oligoadenylate Sus scrofa

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in HeLa-M cell and in Escherichia coli as TEV-cleavable GST fusion proteins Sus scrofa

Crystallization (Commentary)

Crystallization (Comment) Organism
enzyme with bound natural activator 2',5'-oligoadenylate and with and without ADP or the nonhydrolysable ATP mimetic AMP-PNP, X-ray diffraction structure determination and analysis at 2.5 A resolution and small-angle X-ray scattering structure determination and analysis at 3.25 A resolution Sus scrofa

Protein Variants

Protein Variants Comment Organism
K390R the mutation in the kinase ATP binding site of the nezyme results in greatly impaired RNase activity Sus scrofa
K392R the mutation in the kinase ATP binding site of the nezyme results in greatly impaired RNase activity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged wild-type and mutant enzymes from Escherichia coli by glutathione affinity chromatography and TEV-cleavage Sus scrofa

Subunits

Subunits Comment Organism
dimer the dimer configuration of full-length enzyme arises from the intertwining of two promoters through a 155° twisting action across the ANK domain-PK domain junction, which gives rise to the appearance of an exchange of ANK and PK domains between protomers, back-to-back dimer arrangement. Dimerization of the ANK domain is facilitated by a head-to-tail arrangement with concave surfaces facing inward. Kinase domain-ANK domain contacts, overview Homo sapiens
dimer the dimer configuration of full-length enzyme arises from the intertwining of two promoters through a 155° twisting action across the ANK domain-PK domain junction, which gives rise to the appearance of an exchange of ANK and PK domains between protomers, back-to-back dimer arrangement. Dimerization of the ANK domain is facilitated by a head-to-tail arrangement with concave surfaces facing inward. Kinase domain-ANK domain contacts, overview Sus scrofa
More consisting of nine alpha helices with a 19-residue disordered sequence (residues 644-662, harboring a 12-residue porcine-specific insertion) between helices alpha3 and alpha4, RNase domain structure, overview. The ANK domain of porcine RNase L adopts a crescent-shaped structure consisting of a stack of nine ankyrin repeats, each possessing a characteristic loop-helix1-loop-helix2-loop architecture Sus scrofa

Synonyms

Synonyms Comment Organism
RNase L
-
 Homo sapiens
RNase L
-
 Sus scrofa

General Information

General Information Comment Organism
evolution involvement of the pseudokinase domain of the enzyme cofactor sensing, nucleotide binding, dimerization, and ribonuclease functions highlights the evolutionary adaptability of the eukaryotic protein kinase fold Homo sapiens
evolution involvement of the pseudokinase domain of the enzyme cofactor sensing, nucleotide binding, dimerization, and ribonuclease functions highlights the evolutionary adaptability of the eukaryotic protein kinase fold Sus scrofa
additional information involvement of the pseudokinase domain of the enzyme activator sensing, nucleotide binding, dimerization, and ribonuclease functions Homo sapiens
additional information involvement of the pseudokinase domain of the enzyme activator sensing, nucleotide binding, dimerization, and ribonuclease functions Sus scrofa
physiological function RNase L is an ankyrin repeat domain-containing dual endoribonuclease-pseudokinase that is activated by unusual 2',5'-oligoadenylate second messengers and impedes viral infections in higher vertebrates. The enzyme is important in interferon-regulated antiviral innate immunity. Molecular basis for the regulation of the enzyme's antiviral function, overview Homo sapiens
physiological function RNase L is an ankyrin repeat domain-containing dual endoribonuclease-pseudokinase that is activated by unusual 2',5'-oligoadenylate second messengers and impedes viral infections in higher vertebrates. The enzyme is important in interferon-regulated antiviral innate immunity. Molecular basis for the regulation of the enzyme's antiviral function, overview Sus scrofa