1ESG
RESTRICTION ENDONUCLEASE BAMHI BOUND TO A NON-SPECIFIC DNA.
Summary for 1ESG
| Entry DOI | 10.2210/pdb1esg/pdb |
| Related | 1bam 1bhm 2bam 3bam |
| Descriptor | DNA (5'-D(*TP*GP*GP*AP*TP*TP*CP*A)-3'), DNA (5'-D(*TP*GP*AP*AP*TP*CP*CP*A)-3'), TYPE II RESTRICTION ENZYME BAMHI, ... (4 entities in total) |
| Functional Keywords | non-specific dna-protein complex., hydrolase-dna complex, hydrolase/dna |
| Biological source | Bacillus amyloliquefaciens More |
| Total number of polymer chains | 4 |
| Total formula weight | 54056.84 |
| Authors | Viadiu, H.,Aggarwal, A.K. (deposition date: 2000-04-09, release date: 2000-05-31, Last modification date: 2024-02-07) |
| Primary citation | Viadiu, H.,Aggarwal, A.K. Structure of BamHI bound to nonspecific DNA: a model for DNA sliding. Mol.Cell, 5:889-895, 2000 Cited by PubMed Abstract: 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. PubMed: 10882125DOI: 10.1016/S1097-2765(00)80329-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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