1vde

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(New page: 200px<br /><applet load="1vde" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vde, resolution 2.4&Aring;" /> '''PI-SCEI, A HOMING END...)
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'''PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY'''<br />
'''PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1VDE 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=1VDE OCA].
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1VDE 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=1VDE OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Duan, X.]]
[[Category: Duan, X.]]
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[[Category: Quiocho, F.A.]]
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[[Category: Quiocho, F A.]]
[[Category: homing endonuclease]]
[[Category: homing endonuclease]]
[[Category: protein splicing]]
[[Category: protein splicing]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:36:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:34:05 2008''

Revision as of 13:34, 21 February 2008


1vde, resolution 2.4Å

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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.

About this Structure

1VDE 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

Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity., Duan X, Gimble FS, Quiocho FA, Cell. 1997 May 16;89(4):555-64. PMID:9160747

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