1vde: Difference between revisions

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[[Image:1vde.~~gif~~|left|200px]]

[[Image:1vde.png|left|200px]]

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~~'''~~PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY~~'''~~

===PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY===

~~==Overview==~~

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PI-~~Scel is a bifunctional yeast protein that propagates its mobile gene by catalyzing protein splicing and site~~-~~specific DNA double-strand cleavage. Here~~, ~~we report~~ the 2.~~4 A crystal structure of the PI-Scel protein~~. ~~The structure is composed of two separate domains (I and II~~) ~~with novel folds and different functions. Domain I~~, ~~which~~ is ~~elongated and formed largely from seven beta sheets, harbors~~ the ~~N and C termini residues and two His residues that are implicated in protein splicing~~. ~~Domain II, which is compact and is primarily composed of two similar alpha/beta motifs related by local two~~-fold symmetry, contains the putative nuclease active site with a cluster of two acidic residues and one basic residue commonly found in restriction endonucleases. This report presents prototypic structures of domains with single endonuclease and protein splicing active sites.

The line below this paragraph, {{ABSTRACT_PUBMED_9160747}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9160747 is the PubMed ID number.

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==About this Structure==

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[[Category: Homing endonuclease]]

[[Category: Protein splicing]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 12~~:24:25 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:43:44 2008''

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-[[Image:1vde.gif|left|200px]]
+{{Seed}}
+[[Image:1vde.png|left|200px]]
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 {{STRUCTURE_1vde|  PDB=1vde  |  SCENE=  }}
-'''PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY'''
+===PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY===
-==Overview==
+<!--
-PI-Scel is a bifunctional yeast protein that propagates its mobile gene by catalyzing protein splicing and site-specific DNA double-strand cleavage. Here, we report the 2.4 A crystal structure of the PI-Scel protein. The structure is composed of two separate domains (I and II) with novel folds and different functions. Domain I, which is elongated and formed largely from seven beta sheets, harbors the N and C termini residues and two His residues that are implicated in protein splicing. Domain II, which is compact and is primarily composed of two similar alpha/beta motifs related by local two-fold symmetry, contains the putative nuclease active site with a cluster of two acidic residues and one basic residue commonly found in restriction endonucleases. This report presents prototypic structures of domains with single endonuclease and protein splicing active sites.
+The line below this paragraph, {{ABSTRACT_PUBMED_9160747}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9160747 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9160747}}
 ==About this Structure==
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 [[Category: Homing endonuclease]]
 [[Category: Protein splicing]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 12:24:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:43:44 2008''