2ost

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(New page: 200px<br /><applet load="2ost" size="350" color="white" frame="true" align="right" spinBox="true" caption="2ost, resolution 3.100&Aring;" /> '''The structure of a ...)
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==Overview==
==Overview==
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The homing endonuclease I-Ssp6803I causes the insertion of a group I, intron into a bacterial tRNA gene-the only example of an invasive mobile, intron within a bacterial genome. Using a computational fold prediction, mutagenic screen and crystal structure determination, we demonstrate that, this protein is a tetrameric PD-(D/E)-XK endonuclease-a fold normally used, to protect a bacterial genome from invading DNA through the action of, restriction endonucleases. I-Ssp6803I uses its tetrameric assembly to, promote recognition of a single long target site, whereas restriction, endonuclease tetramers facilitate cooperative binding and cleavage of two, short sites. The limited use of the PD-(D/E)-XK nucleases by mobile, introns stands in contrast to their frequent use of LAGLIDADG and HNH, endonucleases-which in turn, are rarely incorporated into, restriction/modification systems.
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The homing endonuclease I-Ssp6803I causes the insertion of a group I intron into a bacterial tRNA gene-the only example of an invasive mobile intron within a bacterial genome. Using a computational fold prediction, mutagenic screen and crystal structure determination, we demonstrate that this protein is a tetrameric PD-(D/E)-XK endonuclease - a fold normally used to protect a bacterial genome from invading DNA through the action of restriction endonucleases. I-Ssp6803I uses its tetrameric assembly to promote recognition of a single long target site, whereas restriction endonuclease tetramers facilitate cooperative binding and cleavage of two short sites. The limited use of the PD-(D/E)-XK nucleases by mobile introns stands in contrast to their frequent use of LAGLIDADG and HNH endonucleases - which in turn, are rarely incorporated into restriction/modification systems.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Synechocystis sp.]]
[[Category: Synechocystis sp.]]
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[[Category: Bonocora, R.P.]]
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[[Category: Bonocora, R P.]]
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[[Category: Shub, D.A.]]
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[[Category: Shub, D A.]]
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[[Category: Stoddard, B.L.]]
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[[Category: Stoddard, B L.]]
[[Category: Zhao, L.]]
[[Category: Zhao, L.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: restriction enzyme fold]]
[[Category: restriction enzyme fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:15:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:22:06 2008''

Revision as of 16:22, 21 February 2008


2ost, resolution 3.100Å

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The structure of a bacterial homing endonuclease : I-Ssp6803I

Overview

The homing endonuclease I-Ssp6803I causes the insertion of a group I intron into a bacterial tRNA gene-the only example of an invasive mobile intron within a bacterial genome. Using a computational fold prediction, mutagenic screen and crystal structure determination, we demonstrate that this protein is a tetrameric PD-(D/E)-XK endonuclease - a fold normally used to protect a bacterial genome from invading DNA through the action of restriction endonucleases. I-Ssp6803I uses its tetrameric assembly to promote recognition of a single long target site, whereas restriction endonuclease tetramers facilitate cooperative binding and cleavage of two short sites. The limited use of the PD-(D/E)-XK nucleases by mobile introns stands in contrast to their frequent use of LAGLIDADG and HNH endonucleases - which in turn, are rarely incorporated into restriction/modification systems.

About this Structure

2OST is a Single protein structure of sequence from Synechocystis sp. with as ligand. Full crystallographic information is available from OCA.

Reference

The restriction fold turns to the dark side: a bacterial homing endonuclease with a PD-(D/E)-XK motif., Zhao L, Bonocora RP, Shub DA, Stoddard BL, EMBO J. 2007 May 2;26(9):2432-42. Epub 2007 Apr 5. PMID:17410205

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