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1gpp
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(New page: 200px<br /><applet load="1gpp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gpp, resolution 1.35Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 14:06, 20 November 2007
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CRYSTAL STRUCTURE OF THE S.CEREVISIAE HOMING ENDONUCLEASE PI-SCEI DOMAIN I
Overview
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.
About this Structure
1GPP is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as H(+)-transporting two-sector ATPase, with EC number 3.6.3.14 Full crystallographic information is available from OCA.
Reference
High resolution crystal structure of domain I of the Saccharomyces cerevisiae homing endonuclease PI-SceI., Werner E, Wende W, Pingoud A, Heinemann U, Nucleic Acids Res. 2002 Sep 15;30(18):3962-71. PMID:12235380
Page seeded by OCA on Tue Nov 20 16:13:28 2007
