1es8

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(New page: 200px<br /><applet load="1es8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1es8, resolution 2.3&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1es8.jpg|left|200px]]<br /><applet load="1es8" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1es8.jpg|left|200px]]<br /><applet load="1es8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1es8, resolution 2.3&Aring;" />
caption="1es8, resolution 2.3&Aring;" />
'''CRYSTAL STRUCTURE OF FREE BGLII'''<br />
'''CRYSTAL STRUCTURE OF FREE BGLII'''<br />
==Overview==
==Overview==
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Restriction endonuclease BglII completely encircles its target DNA, making, contacts to both the major and minor grooves. To allow the DNA to enter, and leave the binding cleft, the enzyme dimer has to rearrange. To, understand how this occurs, we have solved the structure of the free, enzyme at 2.3 A resolution, as a complement to our earlier work on the, BglII-DNA complex. Unexpectedly, the enzyme opens by a dramatic, 'scissor-like' motion, accompanied by a complete rearrangement of the, alpha-helices at the dimer interface. Moreover, within each monomer, a set, of residues--a 'lever'--lowers or raises to alternately sequester or, expose the active site residues. Such an extreme difference in free versus, complexed structures has not been reported for other restriction, endonucleases. This elegant mechanism for capturing DNA may extend to, other enzymes that encircle DNA.
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Restriction endonuclease BglII completely encircles its target DNA, making contacts to both the major and minor grooves. To allow the DNA to enter and leave the binding cleft, the enzyme dimer has to rearrange. To understand how this occurs, we have solved the structure of the free enzyme at 2.3 A resolution, as a complement to our earlier work on the BglII-DNA complex. Unexpectedly, the enzyme opens by a dramatic 'scissor-like' motion, accompanied by a complete rearrangement of the alpha-helices at the dimer interface. Moreover, within each monomer, a set of residues--a 'lever'--lowers or raises to alternately sequester or expose the active site residues. Such an extreme difference in free versus complexed structures has not been reported for other restriction endonucleases. This elegant mechanism for capturing DNA may extend to other enzymes that encircle DNA.
==About this Structure==
==About this Structure==
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1ES8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ACY as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ES8 OCA].
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1ES8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=ACY:'>ACY</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ES8 OCA].
==Reference==
==Reference==
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Aggarwal, A.K.]]
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[[Category: Aggarwal, A K.]]
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[[Category: Lukacs, C.M.]]
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[[Category: Lukacs, C M.]]
[[Category: ACY]]
[[Category: ACY]]
[[Category: restriction endonuclease]]
[[Category: restriction endonuclease]]
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[[Category: uncomplexed]]
[[Category: uncomplexed]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:16:11 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:30:58 2008''

Revision as of 10:30, 21 February 2008


1es8, resolution 2.3Å

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CRYSTAL STRUCTURE OF FREE BGLII

Overview

Restriction endonuclease BglII completely encircles its target DNA, making contacts to both the major and minor grooves. To allow the DNA to enter and leave the binding cleft, the enzyme dimer has to rearrange. To understand how this occurs, we have solved the structure of the free enzyme at 2.3 A resolution, as a complement to our earlier work on the BglII-DNA complex. Unexpectedly, the enzyme opens by a dramatic 'scissor-like' motion, accompanied by a complete rearrangement of the alpha-helices at the dimer interface. Moreover, within each monomer, a set of residues--a 'lever'--lowers or raises to alternately sequester or expose the active site residues. Such an extreme difference in free versus complexed structures has not been reported for other restriction endonucleases. This elegant mechanism for capturing DNA may extend to other enzymes that encircle DNA.

About this Structure

1ES8 is a Single protein structure of sequence from Bacillus subtilis with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of free BglII reveals an unprecedented scissor-like motion for opening an endonuclease., Lukacs CM, Kucera R, Schildkraut I, Aggarwal AK, Nat Struct Biol. 2001 Feb;8(2):126-30. PMID:11175900

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