1GPP

Crystal structure of the S.cerevisiae Homing Endonuclease PI-SceI Domain I

Summary for 1GPP

• Entry DOI: 10.2210/pdb1gpp/pdb
• Related: 1DFA 1VDE
• Descriptor: ENDONUCLEASE PI-SCEI (2 entities in total)
• Functional Keywords: endonuclease, homing, protein splicing
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 1
• Total formula weight: 27034.64

Authors

Werner, E.,Wende, W.,Pingoud, A.,Heinemann, U. (deposition date: 2001-11-07, release date: 2002-09-19, Last modification date: 2023-12-13)

Primary citation

Werner, E.,Wende, W.,Pingoud, A.,Heinemann, U.
High Resolution Crystal Structure of Domain I of the Saccharomyces Cerevisiae Homing Endonuclease Pi-Scei
Nucleic Acids Res., 30:3962-, 2002

PubMed 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.

PubMed: 12235380
DOI: 10.1093/NAR/GKF523

Experimental method

X-RAY DIFFRACTION (1.35 Å)