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Literature summary for 2.7.7.48 extracted from

  • Shatskaya, G.S.; Dmitrieva, T.M.
    Structural organization of viral RNA-dependent RNA polymerases (2013), Biochemistry (Moscow), 78, 231-235.
    View publication on PubMed
Search for more literature for 2.7.7.48

Protein Variants

Protein Variants Comment Organism
G64S mutation of the key structural element of the alpha-helix in poliovirus RdRP, leads to the appearance of virus that reproduced better than the wild-type, the mutation stabilizes the interaction f Gly64 with residues Ala239 and Leu241 of the fingers subdomain Enterovirus C

Organism

Organism UniProt Comment Textmining
Birnaviridae
-
-
-
Enterovirus C
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 a picorna virus
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Foot-and-mouth disease virus
-
-
-
Hepacivirus C
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 a flavivirus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information presence of motif G is important for primer-dependent RNA synthesis but not to affect the binding of the enzyme to the template Hepacivirus C ?
-
 ?
additional information the conservative lysine residue K359 in motif D is a dynamic element whose position inside the polymerase molecule may determine the velocity of the enzymatic reaction Enterovirus C ?
-
 ?
additional information the conservative lysine residue K369 in motif D is a dynamic element whose position inside the polymerase molecule may determine the velocity of the enzymatic reaction Foot-and-mouth disease virus ?
-
 ?
additional information the conservative lysine residue K369 in motif D is a dynamic element whose position inside the polymerase molecule may determine the velocity of the enzymatic reaction Birnaviridae ?
-
 ?

Subunits

Subunits Comment Organism
More structure of the RNA polymerase of poliovirus (1RA6) with subdomains fingers, palm, and thumb. Molecular dynamics simulations Enterovirus C

Synonyms

Synonyms Comment Organism
RDRP
-
 Foot-and-mouth disease virus
RDRP
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 Hepacivirus C
RDRP
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 Enterovirus C
RDRP
-
 Birnaviridae

General Information

General Information Comment Organism
additional information viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. Formation of the active site by palm conservative elements Foot-and-mouth disease virus
additional information viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. Formation of the active site by palm conservative elements, birnaviral RdRP contains a K+-binding site within its palm subdomain. In most known polymerases, the conservative elements are arranged in alphabetical order, but variants with non-canonical sequence in the primarystructure also exist. In this way the polymerases of birnaviruses and some insect viruses possess elements of the active site in the order: C-A-B-D-E-F. Motif F carries conservative basic lysine and arginine residues that may be involved in the binding of RNA polymerase of birnaviruses. In birnavirus polymerases a serine residue located in the fingers subdomain can be subjected to guanidylation that birnavirus RdRP requires for self-priming. The thumb subdomain of birnaviral RdRP is close in size to the latter and also consists of four alpha-helices and small beta-sheet, which interacts with two beta-strands of the palm subdomain. The C-terminal subdomains of birnaviral polymerase represents an extra, expanded region with several alpha-helices not assembled into compact structure, and interact with the thumb subdomain and fingertips Birnaviridae
additional information viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. Formation of the active site by palm conservative elements. Molecular dynamics of hepatitis C virus RdRP, when interacting with the molecule of a specific inhibitor that binds to the thumb subdomain, show that the ligand binding significantly reduces the ability of the polymerase to change its conformation Hepacivirus C
additional information viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. The Gly64 in the polymerase molecule binds through hydrogen with N-terminal Gly1, which, in turn, interacts with the amino acid residues from the fingers subdomain (Ala239 and Leu241). Formation of the active site by palm conservative elements Enterovirus C