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| {{STRUCTURE_1gpp| PDB=1gpp | SCENE= }} | | {{STRUCTURE_1gpp| PDB=1gpp | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF THE S.CEREVISIAE HOMING ENDONUCLEASE PI-SCEI DOMAIN I'''
| | ===CRYSTAL STRUCTURE OF THE S.CEREVISIAE HOMING ENDONUCLEASE PI-SCEI DOMAIN I=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_12235380}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12235380 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12235380}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Homing]] | | [[Category: Homing]] |
| [[Category: Protein splicing]] | | [[Category: Protein splicing]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:51:55 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:40:55 2008'' |
