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Ydc2 protein domain
Protein domain From Wikipedia, the free encyclopedia
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In molecular biology, the protein domain, Ydc2 (also known as SpCce1), is a Holliday junction resolvase from the fission yeast Schizosaccharomyces pombe that is involved in the maintenance of mitochondrial DNA.
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Function
In molecular biology, the Ydc2 domains are enzymes, or in other words biological catalysts, capable of resolving Holliday junctions into separate DNA duplexes by cleaving DNA after 5'-CT-3, and 5'-TT-3, sequences.
Properties
The junction resolving enzymes are very diverse, but have the following properties in common:
- high structure specificity for binding
- metal dependent, sequence specific cleavage activity[1]
Essentially, they are highly specific.
Limiting factors
Furthermore, the cleavage efficiency is affected by:
- strand type (continuous or exchange)
- nucleotide sequence at cleavage site[1]
Structure
This protein domain forms a ribonuclease H fold consisting of two beta sheets and one alpha helix, arranged as a beta-alpha-beta motif. Each beta sheet has five strands, arranged in a 32145 order, with the second strand being antiparallel to the rest.[2]
References
Wikiwand - on
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