1lwt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1lwt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lwt, resolution 3.20&Aring;" /> '''Crystal structure of...)
Line 1: Line 1:
-
[[Image:1lwt.gif|left|200px]]<br /><applet load="1lwt" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1lwt.gif|left|200px]]<br /><applet load="1lwt" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lwt, resolution 3.20&Aring;" />
caption="1lwt, resolution 3.20&Aring;" />
'''Crystal structure of the intein homing endonuclease PI-SceI bound to its substrate DNA (Ca2+ free)'''<br />
'''Crystal structure of the intein homing endonuclease PI-SceI bound to its substrate DNA (Ca2+ free)'''<br />
==Overview==
==Overview==
-
The first X-ray structures of an intein-DNA complex, that of the, two-domain homing endonuclease PI-SceI bound to its 36-base pair DNA, substrate, have been determined in the presence and absence of Ca(2+). The, DNA shows an asymmetric bending pattern, with a major 50 degree bend in, the endonuclease domain and a minor 22 degree bend in the splicing domain, region. Distortions of the DNA bound to the endonuclease domain cause the, insertion of the two cleavage sites in the catalytic center. DNA binding, induces changes in the protein conformation. The two overlapping, non-identical active sites in the endonucleolytic center contain two, Ca(+2) ions that coordinate to the catalytic Asp residues. Structure, analysis indicates that the top strand may be cleaved first.
+
The first X-ray structures of an intein-DNA complex, that of the two-domain homing endonuclease PI-SceI bound to its 36-base pair DNA substrate, have been determined in the presence and absence of Ca(2+). The DNA shows an asymmetric bending pattern, with a major 50 degree bend in the endonuclease domain and a minor 22 degree bend in the splicing domain region. Distortions of the DNA bound to the endonuclease domain cause the insertion of the two cleavage sites in the catalytic center. DNA binding induces changes in the protein conformation. The two overlapping non-identical active sites in the endonucleolytic center contain two Ca(+2) ions that coordinate to the catalytic Asp residues. Structure analysis indicates that the top strand may be cleaved first.
==About this Structure==
==About this Structure==
-
1LWT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LWT OCA].
+
1LWT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LWT OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Gimble, F.S.]]
+
[[Category: Gimble, F S.]]
-
[[Category: Moure, C.M.]]
+
[[Category: Moure, C M.]]
-
[[Category: Quiocho, F.A.]]
+
[[Category: Quiocho, F A.]]
[[Category: endonuclease]]
[[Category: endonuclease]]
[[Category: homing endonuclease]]
[[Category: homing endonuclease]]
Line 21: Line 21:
[[Category: protein-dna complex]]
[[Category: protein-dna complex]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:57:03 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:14 2008''

Revision as of 11:49, 21 February 2008


1lwt, resolution 3.20Å

Drag the structure with the mouse to rotate

Crystal structure of the intein homing endonuclease PI-SceI bound to its substrate DNA (Ca2+ free)

Overview

The first X-ray structures of an intein-DNA complex, that of the two-domain homing endonuclease PI-SceI bound to its 36-base pair DNA substrate, have been determined in the presence and absence of Ca(2+). The DNA shows an asymmetric bending pattern, with a major 50 degree bend in the endonuclease domain and a minor 22 degree bend in the splicing domain region. Distortions of the DNA bound to the endonuclease domain cause the insertion of the two cleavage sites in the catalytic center. DNA binding induces changes in the protein conformation. The two overlapping non-identical active sites in the endonucleolytic center contain two Ca(+2) ions that coordinate to the catalytic Asp residues. Structure analysis indicates that the top strand may be cleaved first.

About this Structure

1LWT is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of the intein homing endonuclease PI-SceI bound to its recognition sequence., Moure CM, Gimble FS, Quiocho FA, Nat Struct Biol. 2002 Oct;9(10):764-70. PMID:12219083

Page seeded by OCA on Thu Feb 21 13:49:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools