Ydc2 protein domain
| Ydc2 protein domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Crystal structure of the yeast mitochondrial Holliday junction resolvase, YDC2 | |||||||||
| Identifiers | |||||||||
| Symbol | Ydc2-catalyst | ||||||||
| Pfam | PF09159 | ||||||||
| Pfam clan | CL0219 | ||||||||
| InterPro | IPR015242 | ||||||||
| SCOP2 | 1kcf / SCOPe / SUPFAM | ||||||||
| CDD | cd00529 | ||||||||
| |||||||||
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.
Function
[edit | edit source]The Ydc2 domains are enzymes (or "biological catalysts") that resolve Holliday junctions into separate DNA duplexes by cleaving DNA after 5'-CT-3, and 5'-TT-3, sequences.
Properties
[edit | edit source]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
[edit | edit source]Furthermore, the cleavage efficiency is affected by:
- strand type (continuous or exchange)
- nucleotide sequence at cleavage site[1]
Structure
[edit | edit source]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]