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| {{STRUCTURE_1r5t| PDB=1r5t | SCENE= }} | | {{STRUCTURE_1r5t| PDB=1r5t | SCENE= }} |
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| '''The Crystal Structure of Cytidine Deaminase CDD1, an Orphan C to U editase from Yeast'''
| | ===The Crystal Structure of Cytidine Deaminase CDD1, an Orphan C to U editase from Yeast=== |
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| ==Overview==
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| Activation-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 line below this paragraph, {{ABSTRACT_PUBMED_15148397}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15148397 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15148397}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Rna editing]] | | [[Category: Rna editing]] |
| [[Category: Zinc dependent deaminase]] | | [[Category: Zinc dependent deaminase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:06:56 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:54:56 2008'' |