The crystal structure of flap endonuclease-1 from Methanococcus jannaschii.
Flap endonuclease-1 (FEN-1), a structure specific nuclease, is an essential enzyme for eukaryotic DNA replication and repair. The crystal structure of FEN-1 from Methanococcus jannaschii, determined at 2.0 A resolution, reveals an active site with two metal ions residing on top of a deep cleft where several conserved acidic residues are clustered. Near the active site, a long flexible loop comprised of many basic and aromatic residues forms a hole large enough to accommodate the DNA substrate. Deletion mutations in this loop significantly decreased the nuclease activity and specificity of FEN-1, suggesting that the loop is critical for recognition and cleavage of the junction between single and double-stranded regions of flap DNA.
Structural Biology Center, Korea Institute of Science & Technology, Seoul, South Korea.
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Hwang
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Baek
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Kim
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Cho
D000595:Amino Acid Sequence; D001665:Binding Sites; D003198:Computer Simulation; D017124:Conserved Sequence; D003461:Crystallography; D004252:DNA Mutational Analysis; D004260:DNA Repair; D004261:DNA Replication; D004706:Endodeoxyribonucleases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D045585:Flap Endonucleases; D008274:Magnesium; D008345:Manganese; D017017:Methanococcus / Q000201:enzymology*; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry; D017384:Sequence Deletion; D017386:Sequence Homology, Amino Acid
D011994:Recombinant Proteins; D008345:Manganese; D004706:Endodeoxyribonucleases; D045585:Flap Endonucleases; D008274:Magnesium