2bam: Difference between revisions
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New page: left|200px<br /><applet load="2bam" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bam, resolution 2.0Å" /> '''RESTRICTION ENDONUCLE... |
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== | ==RESTRICTION ENDONUCLEASE BAMHI COMPLEX WITH DNA AND CALCIUM IONS (PRE-REACTIVE COMPLEX).== | ||
Type II restriction enzymes are characterized by their remarkable | <StructureSection load='2bam' size='340' side='right'caption='[[2bam]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bam]] 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=2BAM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BAM FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=2bam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bam OCA], [https://pdbe.org/2bam PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bam RCSB], [https://www.ebi.ac.uk/pdbsum/2bam PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bam ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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 == | |||
Type II restriction enzymes are characterized by their remarkable specificity and simplicity. They require only divalent metals (such as Mg2+ or Mn2+) as cofactors to catalyze the hydrolysis of DNA. However, most of the structural work on endonucleases has been performed in the absence of metals, leaving unanswered questions about their mechanisms of DNA cleavage. Here we report structures of the endonuclease BamHI-DNA complex, determined in the presence of Mn2+ and Ca2+, that describe the enzyme at different stages of catalysis. Overall, the results support a two-metal mechanism of DNA cleavage for BamHI which is distinct from that of EcoRV. | |||
The role of metals in catalysis by the restriction endonuclease BamHI.,Viadiu H, Aggarwal AK Nat Struct Biol. 1998 Oct;5(10):910-6. PMID:9783752<ref>PMID:9783752</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 2bam" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[BamHI|BamHI]] | |||
*[[Endonuclease 3D structures|Endonuclease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus amyloliquefaciens]] | [[Category: Bacillus amyloliquefaciens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Aggarwal AK]] | |||
[[Category: Aggarwal | [[Category: Viadiu H]] | ||
[[Category: Viadiu | |||
Latest revision as of 07:36, 23 August 2023
RESTRICTION ENDONUCLEASE BAMHI COMPLEX WITH DNA AND CALCIUM IONS (PRE-REACTIVE COMPLEX).
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