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<StructureSection load='1esg' size='340' side='right'caption='[[1esg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1esg' size='340' side='right'caption='[[1esg]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1esg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ESG FirstGlance]. <br>
<table><tr><td colspan='2'>[[1esg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ESG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ESG FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bam|1bam]], [[2bam|2bam]], [[3bam|3bam]], [[1bhm|1bhm]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1esg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esg OCA], [https://pdbe.org/1esg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1esg RCSB], [https://www.ebi.ac.uk/pdbsum/1esg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1esg ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1esg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esg OCA], [https://pdbe.org/1esg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1esg RCSB], [https://www.ebi.ac.uk/pdbsum/1esg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1esg ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/T2BA_BACAM T2BA_BACAM]] Recognizes the double-stranded sequence GGATCC and cleaves after G-1.  
[https://www.uniprot.org/uniprot/T2BA_BACAM T2BA_BACAM] Recognizes the double-stranded sequence GGATCC and cleaves after G-1.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
 
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<ref>PMID:10882125</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1esg" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[BamHI|BamHI]]
*[[BamHI|BamHI]]
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus amyloliquefaciens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Type II site-specific deoxyribonuclease]]
[[Category: Aggarwal AK]]
[[Category: Aggarwal, A K]]
[[Category: Viadiu H]]
[[Category: Viadiu, H]]
[[Category: Hydrolase-dna complex]]
[[Category: Non-specific dna-protein complex]]

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