1u3e

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(New page: 200px<br /><applet load="1u3e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u3e, resolution 2.92&Aring;" /> '''DNA binding and clea...)
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[[Image:1u3e.gif|left|200px]]<br /><applet load="1u3e" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1u3e.gif|left|200px]]<br /><applet load="1u3e" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1u3e, resolution 2.92&Aring;" />
caption="1u3e, resolution 2.92&Aring;" />
'''DNA binding and cleavage by the HNH homing endonuclease I-HmuI'''<br />
'''DNA binding and cleavage by the HNH homing endonuclease I-HmuI'''<br />
==Overview==
==Overview==
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The structure of I-HmuI, which represents the last family of homing, endonucleases without a defining crystallographic structure, has been, determined in complex with its DNA target. A series of diverse protein, structural domains and motifs, contacting sequential stretches of, nucleotide bases, are distributed along the DNA target. I-HmuI contains an, N-terminal domain with a DNA-binding surface found in the I-PpoI homing, endonuclease and an associated HNH/N active site found in the bacterial, colicins, and a C-terminal DNA-binding domain previously observed in the, I-TevI homing endonuclease. The combination and exchange of these features, between protein families indicates that the genetic mobility associated, with homing endonucleases extends to the level of independent structural, domains. I-HmuI provides an unambiguous structural connection between the, His-Cys box endonucleases and the bacterial colicins, supporting the, hypothesis that these enzymes diverged from a common ancestral nuclease.
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The structure of I-HmuI, which represents the last family of homing endonucleases without a defining crystallographic structure, has been determined in complex with its DNA target. A series of diverse protein structural domains and motifs, contacting sequential stretches of nucleotide bases, are distributed along the DNA target. I-HmuI contains an N-terminal domain with a DNA-binding surface found in the I-PpoI homing endonuclease and an associated HNH/N active site found in the bacterial colicins, and a C-terminal DNA-binding domain previously observed in the I-TevI homing endonuclease. The combination and exchange of these features between protein families indicates that the genetic mobility associated with homing endonucleases extends to the level of independent structural domains. I-HmuI provides an unambiguous structural connection between the His-Cys box endonucleases and the bacterial colicins, supporting the hypothesis that these enzymes diverged from a common ancestral nuclease.
==About this Structure==
==About this Structure==
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1U3E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_sp6 Enterobacteria phage sp6] with MN, SR, EDO and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1U3E OCA].
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1U3E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_sp6 Enterobacteria phage sp6] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=SR:'>SR</scene>, <scene name='pdbligand=EDO:'>EDO</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U3E OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Landthaler, M.]]
[[Category: Landthaler, M.]]
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[[Category: Shen, B.W.]]
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[[Category: Shen, B W.]]
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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: EDO]]
[[Category: EDO]]
[[Category: MN]]
[[Category: MN]]
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[[Category: protein-dna complex]]
[[Category: protein-dna complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:49:18 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:20:14 2008''

Revision as of 13:20, 21 February 2008


1u3e, resolution 2.92Å

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DNA binding and cleavage by the HNH homing endonuclease I-HmuI

Overview

The structure of I-HmuI, which represents the last family of homing endonucleases without a defining crystallographic structure, has been determined in complex with its DNA target. A series of diverse protein structural domains and motifs, contacting sequential stretches of nucleotide bases, are distributed along the DNA target. I-HmuI contains an N-terminal domain with a DNA-binding surface found in the I-PpoI homing endonuclease and an associated HNH/N active site found in the bacterial colicins, and a C-terminal DNA-binding domain previously observed in the I-TevI homing endonuclease. The combination and exchange of these features between protein families indicates that the genetic mobility associated with homing endonucleases extends to the level of independent structural domains. I-HmuI provides an unambiguous structural connection between the His-Cys box endonucleases and the bacterial colicins, supporting the hypothesis that these enzymes diverged from a common ancestral nuclease.

About this Structure

1U3E is a Single protein structure of sequence from Enterobacteria phage sp6 with , , and as ligands. Full crystallographic information is available from OCA.

Reference

DNA binding and cleavage by the HNH homing endonuclease I-HmuI., Shen BW, Landthaler M, Shub DA, Stoddard BL, J Mol Biol. 2004 Sep 3;342(1):43-56. PMID:15313606

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