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Literature summary for 3.5.4.B9 extracted from

  • Holden, L.G.; Prochnow, C.; Chang, Y.P.; Bransteitter, R.; Chelico, L.; Sen, U.; Stevens, R.C.; Goodman, M.F.; Chen, X.S.
    Crystal structure of the anti-viral APOBEC3G catalytic domain and functional implications (2008), Nature, 456, 121-124.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.4.B9

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells and in Sf9 insect cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
carboxy-terminal deaminase domain 2 of APOBEC3G (residues 197-380), hanging drop vapor diffusion method, using 100 mM MES, pH 6.5, 40% (w/v) PEG 200, at 18°C Homo sapiens

Protein Variants

Protein Variants Comment Organism
D316R/D317R the mutant shows about 180% deamination activity and about 200% single-stranded DNA binding compared to the wild type enzyme Homo sapiens
F298A the mutant shows about 10% deamination activity compared to the wild type enzyme Homo sapiens
N244A the mutant shows no deamination activity Homo sapiens
R213E the mutant shows about 3% deamination activity compared to the wild type enzyme Homo sapiens
R215E the mutant shows no deamination activity Homo sapiens
R256E the mutant shows about 3% deamination activity compared to the wild type enzyme Homo sapiens
R313E/R320D the mutant shows no deamination activity and about 75% single-stranded DNA binding compared to the wild type enzyme Homo sapiens
R374E/R376D the mutant shows less than 10% deamination activity and about 50% single-stranded DNA binding compared to the wild type enzyme Homo sapiens
W285A the mutant shows no deamination activity Homo sapiens
Y315A the mutant shows no deamination activity Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ contains a zinc atom in the active site Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
cytosine in single-stranded viral DNA + H2O Homo sapiens the full-length enzyme processively deaminates cytidine in two 5'-CCC-3' motifs located on a single-stranded DNA substrate, during one binding event. The full-length enzyme also exerts a 3' to 5' deamination bias by preferentially deaminating the cytidine in the CCC motif near the 5'end of the single-stranded DNA substrate uracil in single-stranded viral DNA + NH3
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9HC16
-
-

Purification (Commentary)

Purification (Comment) Organism
Superdex 75 gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cytosine in single-stranded viral DNA + H2O the full-length enzyme processively deaminates cytidine in two 5'-CCC-3' motifs located on a single-stranded DNA substrate, during one binding event. The full-length enzyme also exerts a 3' to 5' deamination bias by preferentially deaminating the cytidine in the CCC motif near the 5'end of the single-stranded DNA substrate Homo sapiens uracil in single-stranded viral DNA + NH3
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 ?

Synonyms

Synonyms Comment Organism
APOBEC3G
-
 Homo sapiens