1dmu
From Proteopedia
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- | == | + | ==== |
- | <StructureSection load='1dmu' size='340' side='right'caption='[[1dmu]] | + | <StructureSection load='1dmu' size='340' side='right'caption='[[1dmu]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> |
- | </td></tr> | + | </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=1dmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dmu OCA], [https://pdbe.org/1dmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dmu RCSB], [https://www.ebi.ac.uk/pdbsum/1dmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dmu ProSAT]</span></td></tr> |
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- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The crystal structure of the type II restriction endonuclease BglI bound to DNA containing its specific recognition sequence has been determined at 2.2 A resolution. This is the first structure of a restriction endonuclease that recognizes and cleaves an interrupted DNA sequence, producing 3' overhanging ends. BglI is a homodimer that binds its specific DNA sequence with the minor groove facing the protein. Parts of the enzyme reach into both the major and minor grooves to contact the edges of the bases within the recognition half-sites. The arrangement of active site residues is strikingly similar to other restriction endonucleases, but the co-ordination of two calcium ions at the active site gives new insight into the catalytic mechanism. Surprisingly, the core of a BglI subunit displays a striking similarity to subunits of EcoRV and PvuII, but the dimer structure is dramatically different. The BglI-DNA complex demonstrates, for the first time, that a conserved subunit fold can dimerize in more than one way, resulting in different DNA cleavage patterns. | ||
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- | Crystal structure of restriction endonuclease BglI bound to its interrupted DNA recognition sequence.,Newman M, Lunnen K, Wilson G, Greci J, Schildkraut I, Phillips SE EMBO J. 1998 Sep 15;17(18):5466-76. PMID:9736624<ref>PMID:9736624</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1dmu" style="background-color:#fffaf0;"></div> | ||
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- | ==See Also== | ||
- | *[[Endonuclease|Endonuclease]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
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Revision as of 18:30, 10 March 2021
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