PMID:9466941

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Citation

Navaratnam, N, Fujino, T, Bayliss, J, Jarmuz, A, How, A, Richardson, N, Somasekaram, A, Bhattacharya, S, Carter, C and Scott, J (1998) Escherichia coli cytidine deaminase provides a molecular model for ApoB RNA editing and a mechanism for RNA substrate recognition. J. Mol. Biol. 275:695-714

Abstract

ApoB RNA-editing enzyme (APOBEC-1) is a cytidine deaminase. Molecular modeling and mutagenesis show that APOBEC-1 is related in quaternary and tertiary structure to Escherichia coli cytidine deaminase (ECCDA). Both enzymes form a homodimer with composite active sites constructed with contributions from each monomer. Significant gaps are present in the APOBEC-1 sequence, compared to ECCDA. The combined mass of the gaps (10 kDa) matches that for the minimal RNA substrate. Their location in ECCDA suggests how APOBEC-1 can be reshaped to accommodate an RNA substrate. In this model, the asymmetrical binding to one active site of a downstream U (equivalent to the deamination product) helps target the other active site for deamination of the upstream C substrate.

Links

PubMed Online version:10.1006/jmbi.1997.1506

Keywords

Amino Acid Sequence; Apolipoproteins B/genetics; Apolipoproteins B/metabolism; Binding Sites; Cytidine Deaminase/genetics; Cytidine Deaminase/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Models, Molecular; Molecular Sequence Data; RNA Editing; RNA, Bacterial/metabolism; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity

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