1r5t
The Crystal Structure of Cytidine Deaminase CDD1, an Orphan C to U editase from YeastThe Crystal Structure of Cytidine Deaminase CDD1, an Orphan C to U editase from Yeast
Structural highlights
Function[CDD_YEAST] This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedActivation-induced deaminase (AID) uses base deamination for class-switch recombination and somatic hypermutation and is related to the mammalian RNA-editing enzyme apolipoprotein B editing catalytic subunit 1 (APOBEC-1). CDD1 is a yeast ortholog of APOBEC-1 that exhibits cytidine deaminase and RNA-editing activity. Here, we present the crystal structure of CDD1 at 2.0-A resolution and its use in comparative modeling of APOBEC-1 and AID. The models explain dimerization and the need for trans-acting loops that contribute to active site formation. Substrate selectivity appears to be regulated by a central active site "flap" whose size and flexibility accommodate large substrates in contrast to deaminases of pyrimidine metabolism that bind only small nucleosides or free bases. Most importantly, the results suggested both AID and APOBEC-1 are equally likely to bind single-stranded DNA or RNA, which has implications for the identification of natural AID targets. The structure of a yeast RNA-editing deaminase provides insight into the fold and function of activation-induced deaminase and APOBEC-1.,Xie K, Sowden MP, Dance GS, Torelli AT, Smith HC, Wedekind JE Proc Natl Acad Sci U S A. 2004 May 25;101(21):8114-9. Epub 2004 May 17. PMID:15148397[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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