1esg

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(New page: 200px<br /><applet load="1esg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1esg, resolution 1.90&Aring;" /> '''RESTRICTION ENDONUCL...)
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[[Image:1esg.gif|left|200px]]<br /><applet load="1esg" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1esg, resolution 1.90&Aring;" />
caption="1esg, resolution 1.90&Aring;" />
'''RESTRICTION ENDONUCLEASE BAMHI BOUND TO A NON-SPECIFIC DNA.'''<br />
'''RESTRICTION ENDONUCLEASE BAMHI BOUND TO A NON-SPECIFIC DNA.'''<br />
==Overview==
==Overview==
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The central problem faced by DNA binding proteins is how to select the, correct DNA sequence from the sea of nonspecific sequences in a cell. The, problem is particularly acute for bacterial restriction enzymes because, cleavage at an incorrect DNA site could be lethal. To understand the basis, of this selectivity, we report here the crystal structure of endonuclease, BamHI bound to noncognate DNA. We show that, despite only a single base, pair change in the recognition sequence, the enzyme adopts an open, configuration that is on the pathway between free and specifically bound, forms of the enzyme. Surprisingly, the DNA drops out of the binding cleft, with a total loss of base-specific and backbone contacts. Taken together, the structure provides a remarkable snapshot of an enzyme poised for, linear diffusion (rather than cleavage) along the DNA.
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The central problem faced by DNA binding proteins is how to select the correct DNA sequence from the sea of nonspecific sequences in a cell. The problem is particularly acute for bacterial restriction enzymes because cleavage at an incorrect DNA site could be lethal. To understand the basis of this selectivity, we report here the crystal structure of endonuclease BamHI bound to noncognate DNA. We show that, despite only a single base pair change in the recognition sequence, the enzyme adopts an open configuration that is on the pathway between free and specifically bound forms of the enzyme. Surprisingly, the DNA drops out of the binding cleft with a total loss of base-specific and backbone contacts. Taken together, the structure provides a remarkable snapshot of an enzyme poised for linear diffusion (rather than cleavage) along the DNA.
==About this Structure==
==About this Structure==
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1ESG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Active as [http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ESG OCA].
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1ESG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Active as [http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESG OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Type II site-specific deoxyribonuclease]]
[[Category: Type II site-specific deoxyribonuclease]]
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[[Category: Aggarwal, A.K.]]
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[[Category: Aggarwal, A K.]]
[[Category: Viadiu, H.]]
[[Category: Viadiu, H.]]
[[Category: non-specific dna-protein complex.]]
[[Category: non-specific dna-protein complex.]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:16:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:31:01 2008''

Revision as of 10:31, 21 February 2008


1esg, resolution 1.90Å

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RESTRICTION ENDONUCLEASE BAMHI BOUND TO A NON-SPECIFIC DNA.

Overview

The central problem faced by DNA binding proteins is how to select the correct DNA sequence from the sea of nonspecific sequences in a cell. The problem is particularly acute for bacterial restriction enzymes because cleavage at an incorrect DNA site could be lethal. To understand the basis of this selectivity, we report here the crystal structure of endonuclease BamHI bound to noncognate DNA. We show that, despite only a single base pair change in the recognition sequence, the enzyme adopts an open configuration that is on the pathway between free and specifically bound forms of the enzyme. Surprisingly, the DNA drops out of the binding cleft with a total loss of base-specific and backbone contacts. Taken together, the structure provides a remarkable snapshot of an enzyme poised for linear diffusion (rather than cleavage) along the DNA.

About this Structure

1ESG is a Single protein structure of sequence from Bacillus amyloliquefaciens. Active as Type II site-specific deoxyribonuclease, with EC number 3.1.21.4 Full crystallographic information is available from OCA.

Reference

Structure of BamHI bound to nonspecific DNA: a model for DNA sliding., Viadiu H, Aggarwal AK, Mol Cell. 2000 May;5(5):889-95. PMID:10882125

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