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 3.100Å" /> '''The structure of a ...)
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Revision as of 13:15, 23 January 2008
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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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