1KCF

Crystal Structure of the Yeast Mitochondrial Holliday Junction Resolvase, Ydc2

Summary for 1KCF

• Entry DOI: 10.2210/pdb1kcf/pdb
• Descriptor: HYPOTHETICAL 30.2 KD PROTEIN C25G10.02 IN CHROMOSOME I, SULFATE ION (3 entities in total)
• Functional Keywords: beta-alpha-beta motif, ruvc resolvase family, hydrolase
• Biological source: Schizosaccharomyces pombe (fission yeast)
• Cellular location: Mitochondrion: Q10423
• Total number of polymer chains: 2
• Total formula weight: 60687.71

Authors

Ceschini, S.,Keeley, A.,McAlister, M.S.B.,Oram, M.,Phelan, J.,Pearl, L.H.,Tsaneva, I.R.,Barrett, T.E. (deposition date: 2001-11-08, release date: 2001-11-28, Last modification date: 2024-02-07)

Primary citation

Ceschini, S.,Keeley, A.,McAlister, M.S.,Oram, M.,Phelan, J.,Pearl, L.H.,Tsaneva, I.R.,Barrett, T.E.
Crystal structure of the fission yeast mitochondrial Holliday junction resolvase Ydc2.
EMBO J., 20:6601-6611, 2001

PubMed Abstract: Resolution of Holliday junctions into separate DNA duplexes requires enzymatic cleavage of an equivalent strand from each contributing duplex at or close to the point of strand exchange. Diverse Holliday junction-resolving enzymes have been identified in bacteria, bacteriophages, archaea and pox viruses, but the only eukaryotic examples identified so far are those from fungal mitochondria. We have now determined the crystal structure of Ydc2 (also known as SpCce1), a Holliday junction resolvase from the fission yeast Schizosaccharomyces pombe that is involved in the maintenance of mitochondrial DNA. This first structure of a eukaryotic Holliday junction resolvase confirms a distant evolutionary relationship to the bacterial RuvC family, but reveals structural features which are unique to the eukaryotic enzymes. Detailed analysis of the dimeric structure suggests mechanisms for junction isomerization and communication between the two active sites, and together with site-directed mutagenesis identifies residues involved in catalysis.

PubMed: 11726496
DOI: 10.1093/emboj/20.23.6601

Experimental method

X-RAY DIFFRACTION (2.3 Å)