1es8

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[[Image:1es8.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of free BglII==
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|PDB= 1es8 |SIZE=350|CAPTION= <scene name='initialview01'>1es8</scene>, resolution 2.3&Aring;
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<StructureSection load='1es8' size='340' side='right'caption='[[1es8]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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<table><tr><td colspan='2'>[[1es8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ES8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ES8 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1es8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1es8 OCA], [https://pdbe.org/1es8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1es8 RCSB], [https://www.ebi.ac.uk/pdbsum/1es8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1es8 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1dfm|1DFM]], [[1d2i|1D2I]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1es8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1es8 OCA], [http://www.ebi.ac.uk/pdbsum/1es8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1es8 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/T2B2_BACIU T2B2_BACIU] Recognizes the double-stranded sequence AGATCT and cleaves after A-1.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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'''CRYSTAL STRUCTURE OF FREE BGLII'''
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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<ref>PMID:11175900</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1es8" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Endonuclease 3D structures|Endonuclease 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1ES8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ES8 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11175900 11175900]
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[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Aggarwal, A K.]]
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[[Category: Aggarwal AK]]
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[[Category: Lukacs, C M.]]
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[[Category: Lukacs CM]]
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[[Category: restriction endonuclease]]
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[[Category: restriction enzyme]]
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[[Category: uncomplexed]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:08:36 2008''
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Current revision

Crystal structure of free BglII

PDB ID 1es8

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