2p0j

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(New page: 200px<br /><applet load="2p0j" size="350" color="white" frame="true" align="right" spinBox="true" caption="2p0j, resolution 2.100&Aring;" /> '''Structure of restri...)
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==Overview==
==Overview==
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DNA recognition by proteins is essential for specific expression of genes, in a living organism. En route to a target DNA site, a protein will often, sample noncognate DNA sites through nonspecific protein-DNA interactions, resulting in a variety of conformationally different binding states. We, present here the crystal structure of endonuclease BstYI bound to a, noncognate DNA. Surprisingly, the structure reveals the enzyme in a, "hemispecific" binding state on the pathway between nonspecific and, specific recognition. A single base pair change in the DNA abolishes, binding of only one monomer, with the second monomer bound specifically., We show that the enzyme binds essentially as a rigid body, and that one, end of the DNA is accommodated loosely in the binding cleft while the, other end is held tightly. Another intriguing feature of the structure is, Ser172, which has a dual role in establishing nonspecific and specific, contacts. Taken together, the structure provides a snapshot of an enzyme, in a "paused" intermediate state that may be part of a more general, mechanism of scanning DNA.
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DNA recognition by proteins is essential for specific expression of genes in a living organism. En route to a target DNA site, a protein will often sample noncognate DNA sites through nonspecific protein-DNA interactions, resulting in a variety of conformationally different binding states. We present here the crystal structure of endonuclease BstYI bound to a noncognate DNA. Surprisingly, the structure reveals the enzyme in a "hemispecific" binding state on the pathway between nonspecific and specific recognition. A single base pair change in the DNA abolishes binding of only one monomer, with the second monomer bound specifically. We show that the enzyme binds essentially as a rigid body, and that one end of the DNA is accommodated loosely in the binding cleft while the other end is held tightly. Another intriguing feature of the structure is Ser172, which has a dual role in establishing nonspecific and specific contacts. Taken together, the structure provides a snapshot of an enzyme in a "paused" intermediate state that may be part of a more general mechanism of scanning DNA.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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BstYI Bound to Noncognate DNA Reveals a "Hemispecific" Complex: Implications for DNA Scanning., Townson SA, Samuelson JC, Bao Y, Xu SY, Aggarwal AK, Structure. 2007 Apr;15(4):449-59. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17437717 17437717]
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BstYI bound to noncognate DNA reveals a "hemispecific" complex: implications for DNA scanning., Townson SA, Samuelson JC, Bao Y, Xu SY, Aggarwal AK, Structure. 2007 Apr;15(4):449-59. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17437717 17437717]
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Aggarwal, A.K.]]
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[[Category: Aggarwal, A K.]]
[[Category: Bao, Y.]]
[[Category: Bao, Y.]]
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[[Category: Samuelson, J.C.]]
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[[Category: Samuelson, J C.]]
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[[Category: Townson, S.A.]]
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[[Category: Townson, S A.]]
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[[Category: Xu, S.Y.]]
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[[Category: Xu, S Y.]]
[[Category: dna recognition]]
[[Category: dna recognition]]
[[Category: restriction endonuclease]]
[[Category: restriction endonuclease]]
[[Category: scanning]]
[[Category: scanning]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:28:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:24:38 2008''

Revision as of 16:24, 21 February 2008


2p0j, resolution 2.100Å

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Structure of restriction endonuclease BstYI bound to non-cognate DNA

Overview

DNA recognition by proteins is essential for specific expression of genes in a living organism. En route to a target DNA site, a protein will often sample noncognate DNA sites through nonspecific protein-DNA interactions, resulting in a variety of conformationally different binding states. We present here the crystal structure of endonuclease BstYI bound to a noncognate DNA. Surprisingly, the structure reveals the enzyme in a "hemispecific" binding state on the pathway between nonspecific and specific recognition. A single base pair change in the DNA abolishes binding of only one monomer, with the second monomer bound specifically. We show that the enzyme binds essentially as a rigid body, and that one end of the DNA is accommodated loosely in the binding cleft while the other end is held tightly. Another intriguing feature of the structure is Ser172, which has a dual role in establishing nonspecific and specific contacts. Taken together, the structure provides a snapshot of an enzyme in a "paused" intermediate state that may be part of a more general mechanism of scanning DNA.

About this Structure

2P0J is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

Reference

BstYI bound to noncognate DNA reveals a "hemispecific" complex: implications for DNA scanning., Townson SA, Samuelson JC, Bao Y, Xu SY, Aggarwal AK, Structure. 2007 Apr;15(4):449-59. PMID:17437717

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