Literature summary for 3.4.22.29 extracted from

Ling, H.; Yang, P.; Hou, H.; Sun, Y.
Structural view of the 2A protease from human rhinovirus C15 (2018), Acta Crystallogr. Sect. F, 74, 255-261 .

Search for more literature for 3.4.22.29

Cloned(Commentary)

Cloned (Comment)	Organism
sequence comparisons, recombinant expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)	rhinovirus C15

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme, hanging-drop vapour diffusion method, mixing of 200 nl of 10 mg/ml protein in 20 mM HEPES, pH 7.0, 50 mM NaCl, and 10% glycerol, with 200 nl of reservoir solution containing 0.2 M potassium chloride, 0.1 M magnesium acetate tetrahydrate, 0.05 M sodium cacodylate, and 10% PEG 8000, equilibration against 0.1 ml of reservoir solution, 16°C, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement using the structure of 2Apro from coxsackievirus A16 (CVA16) as the search model	rhinovirus C15

Crystallization (Comment)

Organism

purified recombinant enzyme, hanging-drop vapour diffusion method, mixing of 200 nl of 10 mg/ml protein in 20 mM HEPES, pH 7.0, 50 mM NaCl, and 10% glycerol, with 200 nl of reservoir solution containing 0.2 M potassium chloride, 0.1 M magnesium acetate tetrahydrate, 0.05 M sodium cacodylate, and 10% PEG 8000, equilibration against 0.1 ml of reservoir solution, 16°C, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular replacement using the structure of 2Apro from coxsackievirus A16 (CVA16) as the search model

rhinovirus C15

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	the enzyme structure contains a conserved Zn2+-binding site	rhinovirus C15

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
human eukaryotic translation initiation factor 4 G I + H2O	rhinovirus C15	human eIF4GI	?	-	?
human eukaryotic translation initiation factor 4 G II + H2O	rhinovirus C15	human eIF4GII	?	-	?

Organism

Organism	UniProt	Comment	Textmining
rhinovirus C15	A0A2P1DXU1	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant GST-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, anion exchange chromatography, and gel filtration	rhinovirus C15

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
human eukaryotic translation initiation factor 4 G I + H2O	human eIF4GI	rhinovirus C15	?	-	?
human eukaryotic translation initiation factor 4 G II + H2O	human eIF4GII	rhinovirus C15	?	-	?

Subunits

Subunits	Comment	Organism
More	HRV-C15 2Apro consists of two domains: an N-terminal domain comprising of a four-stranded sheet (bI2, cI, eI2 and fI) and a C-terminal domain made up of a six-stranded beta-barrel (aII, bII1, cII2, dII, eII and fII). The N-terminal domain is linked to the C-terminal domain by a long inter-domain loop (residues 40-56). Within the N-terminal domain, a helical turn (Ala17-Leu19) connects cI to eI2. In the C-terminal domain, an antiparallel beta-hairpin, formed by the bII2 and cII1 strands, is located next to the six-stranded beta-barrel. Furthermore, this beta-hairpin also makes close contacts with residues from the N-terminal domain. Three highly conserved residues, His18, Asp34 and Cys105, found in 2Apro from all enteroviruses, form the active site of HRV-C15 2Apro	rhinovirus C15

Synonyms

Synonyms	Comment	Organism
2A protease	-	rhinovirus C15
2Apro	-	rhinovirus C15
HRVC15 2Apro	-	rhinovirus C15

General Information

General Information	Comment	Organism
additional information	the enzyme structure contains a conserved His-Asp-Cys catalytic triad and a Zn2+-binding site. Comparison with other 2Apro structures from enteroviruses reveals that the substrate-binding cleft of 2Apro from HRV-C15 exhibits a more open conformation, which presumably favours substrate binding, structure comparisons, overview	rhinovirus C15
physiological function	the 2A protease (2Apro) of human rhinoviruses (HRVs) plays important roles in the propagation of the virus and the modulation of host signal pathways to facilitate viral replication. The 2A protease (2Apro) specifically cleaves homologues of the human eukaryotic initiation factors eIF4GI and eIF4GII, which are required for cap-dependent mRNA translation by the ribosome. EIF4G is part of the initiation-factor complex eIF4F, which comprises the unwinding protease eIF4A and the cap-binding protein eIF4E. The complex recruits capped cellular mRNA to the ribosome for translation. Cleavage of eIF4G by HRV 2Apro impairs this process and shuts down cap-dependent translation of mRNA. Since the initiation of protein synthesis by picornaviruses is not cap-dependent, but requires the internal ribosome-entry site (IRES) present in the 5'-UTR of the picornavirus mRNA, shutting down the host cap-dependent translation machinery does not affect the synthesis of picornavirus proteins	rhinovirus C15