1gpp: Difference between revisions

Revision as of 13:52, 21 February 2008

CRYSTAL STRUCTURE OF THE S.CEREVISIAE HOMING ENDONUCLEASE PI-SCEI DOMAIN I

OverviewOverview

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 StructureAbout 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.

ReferenceReference

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 Thu Feb 21 12:52:40 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1gpp.gif|left|200px]]<br /><applet load="1gpp" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1gpp.gif|left|200px]]<br /><applet load="1gpp" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1gpp, resolution 1.35&Aring;" />
 '''CRYSTAL STRUCTURE OF THE S.CEREVISIAE HOMING ENDONUCLEASE PI-SCEI DOMAIN I'''<br />
 ==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.
+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==
-GPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GPP OCA].
+GPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Active as [http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GPP OCA].
 ==Reference==
@@ Line 22: / Line 22: @@
 [[Category: protein splicing]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:13:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:52:40 2008''