1bgb

</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=1bgb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bgb OCA], [https://pdbe.org/1bgb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bgb RCSB], [https://www.ebi.ac.uk/pdbsum/1bgb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bgb ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The 2.1-A cocrystal structure of EcoRV endonuclease bound to 5'-CGGGATATCCC, in a crystal lattice isomorphous with the cocrystallized undecamer 5'-AAAGATATCTT previously determined, shows novel base recognition in the major groove of the DNA flanking the GATATC target site. Lys104 of the enzyme interacts through water molecules with the exocyclic N-4 amino groups of flanking cytosines. Steric exclusion of water molecule-binding sites by the 5-methyl group of thymine drives the adoption of alternative water-mediated contacts with AT versus GC flanks. This structure provides a rare example of structural adaptability in the recognition of different DNA sequences by a protein and suggests preferred strategies for the expansion of target site specificity by EcoRV.

Recognition of flanking DNA sequences by EcoRV endonuclease involves alternative patterns of water-mediated contacts.,Horton NC, Perona JJ J Biol Chem. 1998 Aug 21;273(34):21721-9. PMID:9705308<ref>PMID:9705308</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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