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High resolution crystal structure of domain I of the Saccharomyces cerevisiae homing endonuclease PI-SceI

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Item Type:Article
Title:High resolution crystal structure of domain I of the Saccharomyces cerevisiae homing endonuclease PI-SceI
Creators Name:Werner, E. and Wende, W. and Pingoud, A. and Heinemann, U.
Abstract:The homing endonuclease PI-SceI from Saccharo myces cerevisiae consists of two domains. The protein splicing domain I catalyzes the excision of the mature endonuclease (intein) from a precursor protein and the religation of the flanking amino acid sequences (exteins) to a functional protein. Furthermore, domain I is involved in binding and recognition of the specific DNA substrate. Domain II of PI-SceI, the endonuclease domain, which is structurally homologous to other homing endonucleases from the LAGLIDADG family, harbors the endonucleolytic center of PI-SceI, which in vivo initiates the homing process by introducing a double-strand cut in the approximately 35 bp recognition sequence. At 1.35 A resolution, the crystal structure of PI-SceI domain I provides a detailed view of the part of the protein that is responsible for tight and specific DNA binding. A geometry-based docking of the 75 degrees bent recognition sequence to the full-length protein implies a conformational change or hinge movement of a subdomain of domain I, the tongs part, that is predicted to reach into the major groove near base pairs +16 to +18.
Keywords:Binding Sites, X-Ray Crystallography, Endodeoxyribonucleases, Fungal Proteins, Molecular Models, Protein Conformation, Protein Splicing, Tertiary Protein Structure, Proton-Translocating AT, Pases, Saccharomyces Cerevisiae Proteins
Source:Nucleic Acids Research
Publisher:Oxford University Press
Page Range:3962-3971
Date:15 September 2002
Official Publication:https://doi.org/10.1093/nar/gkf523
PubMed:View item in PubMed

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