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3.5.4.38: single-stranded DNA cytosine deaminase

This is an abbreviated version!
For detailed information about single-stranded DNA cytosine deaminase, go to the full flat file.

Word Map on EC 3.5.4.38

Reaction

cytosine in single-stranded DNA
+
H2O
=
uracil in single-stranded DNA
 +
NH3

Synonyms

A3F, activation-induced cytidine deaminase, activation-induced deaminase, AICDA, AID, APOBEC3A, APOBEC3B, APOBEC3C, APOBEC3D, APOBEC3F, APOBEC3G, APOBEC3H, APOBEC3Z1, CDA1, single-stranded (ss)DNA deoxycytidine deaminase, ssDNA cytidine deaminase

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.4 In cyclic amidines
                3.5.4.38 single-stranded DNA cytosine deaminase

Crystallization

Crystallization on EC 3.5.4.38 - single-stranded DNA cytosine deaminase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion technique at 4°C, crystal structure of enzyme variant AIDv(DELTA15), at 2.8 A resolution
generation of a panel of free or DNA-bound AID models based on eight recently resolved APOBEC isoform structures. The majority of AID:DNA complexes would be inactive due to substrate binding such that a cytidine is not positioned for deamination. Most AID conformations exhibit fully or partially occluded catalytic pockets
generation of a panel of free or DNA-bound AID models based on eight resolved APOBEC structures. The majority of AID:DNA complexes would be inactive due to substrate binding such that a cytidine is not positioned for deamination. Most AID conformations exhibit fully or partially occluded catalytic pockets
hanging drop vapor diffusion method
hanging drop vapor diffusion method, APOBEC3B catalytic domain crystal structures including a dCMP-bound form
modeling of structure. Residue Arg211 in loop 1 is the gatekeeper coordinating DNA. ssDNA binds to the C-terminal domain in a U-shape, and loop 1 undergoes major conformational changes to open up the active site for DNA binding. Residue D314 defines substrate specificity for thymidine over cytidine at -1 position. An auto-inhibited conformation in the C-terminal domain restricts access and binding of DNA to the active site
sitting drop vapor diffusion method at 4°C, crystal structure of the catalytic domain of HIV-1 restriction factor APOBEC3G in complex with ssDNA at 1.86 A resolution
sitting drop vapor-diffusion method, crystal structure of the C-terminal catalytic domain of the enzyme (APOBEC3F) in complex with a 10 nucleotide ssDNA composed of a poly-thymine sequence