1BGB
ECORV ENDONUCLEASE COMPLEX WITH 5'-CGGGATATCCC DNA
Summary for 1BGB
| Entry DOI | 10.2210/pdb1bgb/pdb |
| Descriptor | DNA (5'-D(*CP*GP*GP*GP*AP*TP*AP*TP*CP*CP*C)-3'), ECORV ENDONUCLEASE (3 entities in total) |
| Functional Keywords | complex (endonuclease-dna), hydrolase-dna complex, hydrolase/dna |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 63786.69 |
| Authors | Perona, J.,Horton, N.C. (deposition date: 1998-05-28, release date: 1998-10-28, Last modification date: 2024-02-07) |
| Primary citation | Horton, N.C.,Perona, J.J. Recognition of flanking DNA sequences by EcoRV endonuclease involves alternative patterns of water-mediated contacts. J.Biol.Chem., 273:21721-21729, 1998 Cited by PubMed Abstract: 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. PubMed: 9705308DOI: 10.1074/jbc.273.34.21721 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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