1m5x

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(New page: 200px<br /><applet load="1m5x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m5x, resolution 2.25&Aring;" /> '''Crystal structure of...)
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[[Image:1m5x.gif|left|200px]]<br /><applet load="1m5x" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1m5x, resolution 2.25&Aring;" />
caption="1m5x, resolution 2.25&Aring;" />
'''Crystal structure of the homing endonuclease I-MsoI bound to its DNA substrate'''<br />
'''Crystal structure of the homing endonuclease I-MsoI bound to its DNA substrate'''<br />
==Overview==
==Overview==
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Homing endonucleases are highly specific catalysts of DNA strand breaks, that induce the transposition of mobile intervening sequences containing, the endonuclease open reading frame. These enzymes recognize long DNA, targets while tolerating individual sequence polymorphisms within those, sites. Sequences of the homing endonucleases themselves diversify to a, great extent after founding intron invasion events, generating highly, divergent enzymes that recognize similar target sequences. Here, we, visualize the mechanism of flexible DNA recognition and the pattern of, structural divergence displayed by two homing endonuclease isoschizomers., We determined structures of I-CreI bound to two DNA target sites that, differ at eight of 22 base-pairs, and the structure of an isoschizomer, I-MsoI, bound to a nearly identical DNA target site. This study, illustrates several principles governing promiscuous base-pair recognition, by DNA-binding proteins, and demonstrates that the isoschizomers display, strikingly different protein/DNA contacts. The structures allow us to, determine the information content at individual positions in the binding, site as a function of the distribution of direct and water-mediated, contacts to nucleotide bases, and provide an evolutionary snapshot of, endonucleases at an early stage of divergence in their target specificity.
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Homing endonucleases are highly specific catalysts of DNA strand breaks that induce the transposition of mobile intervening sequences containing the endonuclease open reading frame. These enzymes recognize long DNA targets while tolerating individual sequence polymorphisms within those sites. Sequences of the homing endonucleases themselves diversify to a great extent after founding intron invasion events, generating highly divergent enzymes that recognize similar target sequences. Here, we visualize the mechanism of flexible DNA recognition and the pattern of structural divergence displayed by two homing endonuclease isoschizomers. We determined structures of I-CreI bound to two DNA target sites that differ at eight of 22 base-pairs, and the structure of an isoschizomer, I-MsoI, bound to a nearly identical DNA target site. This study illustrates several principles governing promiscuous base-pair recognition by DNA-binding proteins, and demonstrates that the isoschizomers display strikingly different protein/DNA contacts. The structures allow us to determine the information content at individual positions in the binding site as a function of the distribution of direct and water-mediated contacts to nucleotide bases, and provide an evolutionary snapshot of endonucleases at an early stage of divergence in their target specificity.
==About this Structure==
==About this Structure==
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1M5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Monomastix_sp. Monomastix sp.] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M5X OCA].
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1M5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Monomastix_sp. Monomastix sp.] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5X OCA].
==Reference==
==Reference==
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[[Category: Chevalier, B.]]
[[Category: Chevalier, B.]]
[[Category: Lemieux, C.]]
[[Category: Lemieux, C.]]
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[[Category: Monnat, R.J.]]
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[[Category: Monnat, R J.]]
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[[Category: Stoddard, B.L.]]
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[[Category: Stoddard, B L.]]
[[Category: Turmel, M.]]
[[Category: Turmel, M.]]
[[Category: CA]]
[[Category: CA]]
[[Category: laglidadg]]
[[Category: laglidadg]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:49:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:47 2008''

Revision as of 11:51, 21 February 2008


1m5x, resolution 2.25Å

Drag the structure with the mouse to rotate

Crystal structure of the homing endonuclease I-MsoI bound to its DNA substrate

Overview

Homing endonucleases are highly specific catalysts of DNA strand breaks that induce the transposition of mobile intervening sequences containing the endonuclease open reading frame. These enzymes recognize long DNA targets while tolerating individual sequence polymorphisms within those sites. Sequences of the homing endonucleases themselves diversify to a great extent after founding intron invasion events, generating highly divergent enzymes that recognize similar target sequences. Here, we visualize the mechanism of flexible DNA recognition and the pattern of structural divergence displayed by two homing endonuclease isoschizomers. We determined structures of I-CreI bound to two DNA target sites that differ at eight of 22 base-pairs, and the structure of an isoschizomer, I-MsoI, bound to a nearly identical DNA target site. This study illustrates several principles governing promiscuous base-pair recognition by DNA-binding proteins, and demonstrates that the isoschizomers display strikingly different protein/DNA contacts. The structures allow us to determine the information content at individual positions in the binding site as a function of the distribution of direct and water-mediated contacts to nucleotide bases, and provide an evolutionary snapshot of endonucleases at an early stage of divergence in their target specificity.

About this Structure

1M5X is a Single protein structure of sequence from Monomastix sp. with as ligand. Full crystallographic information is available from OCA.

Reference

Flexible DNA target site recognition by divergent homing endonuclease isoschizomers I-CreI and I-MsoI., Chevalier B, Turmel M, Lemieux C, Monnat RJ Jr, Stoddard BL, J Mol Biol. 2003 May 30;329(2):253-69. PMID:12758074

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