The crystal structure of flap endonuclease-1 from Methanococcus jannaschii

Kwang Yeon Hwang; Kyuwon Baek; Hye Yeon Kim; Yunje Cho

doi:10.1038/1406

The crystal structure of flap endonuclease-1 from Methanococcus jannaschii

Kwang Yeon Hwang, Kyuwon Baek, Hye Yeon Kim, Yunje Cho

Research output: Contribution to journal › Article › peer-review

149 Citations (Scopus)

Abstract

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 Å 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.

Original language	English
Pages (from-to)	707-713
Number of pages	7
Journal	Nature Structural and Molecular Biology
Volume	5
Issue number	8
DOIs	https://doi.org/10.1038/1406
Publication status	Published - 1998 Aug

Bibliographical note

Funding Information:
We are grateful to M. S. Park (Los Alamos National Lab), S. S. Kim, E. Kim (L.G. Biotech) for their invaluable comments. We thanks to K. W. Bae and C. S. Cho for technical assistance. This work was supported by Biotech 2000 program from MOST and KIST 2000 program from KIST.

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1038/1406

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title = "The crystal structure of flap endonuclease-1 from Methanococcus jannaschii",

abstract = "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 {\AA} 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.",

author = "Hwang, {Kwang Yeon} and Kyuwon Baek and Kim, {Hye Yeon} and Yunje Cho",

note = "Funding Information: We are grateful to M. S. Park (Los Alamos National Lab), S. S. Kim, E. Kim (L.G. Biotech) for their invaluable comments. We thanks to K. W. Bae and C. S. Cho for technical assistance. This work was supported by Biotech 2000 program from MOST and KIST 2000 program from KIST.",

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N1 - Funding Information: We are grateful to M. S. Park (Los Alamos National Lab), S. S. Kim, E. Kim (L.G. Biotech) for their invaluable comments. We thanks to K. W. Bae and C. S. Cho for technical assistance. This work was supported by Biotech 2000 program from MOST and KIST 2000 program from KIST.

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N2 - 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 Å 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.

AB - 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 Å 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.

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The crystal structure of flap endonuclease-1 from Methanococcus jannaschii

Abstract

Bibliographical note

ASJC Scopus subject areas

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