1ES8
Crystal structure of free BglII
Summary for 1ES8
| Entry DOI | 10.2210/pdb1es8/pdb |
| Related | 1D2I 1DFM |
| Descriptor | RESTRICTION ENDONUCLEASE BGLII, ACETIC ACID (3 entities in total) |
| Functional Keywords | restriction endonuclease, restriction enzyme, uncomplexed, hydrolase |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 1 |
| Total formula weight | 26091.81 |
| Authors | Lukacs, C.M.,Aggarwal, A.K. (deposition date: 2000-04-07, release date: 2001-01-17, Last modification date: 2024-10-30) |
| Primary citation | Lukacs, C.M.,Kucera, R.,Schildkraut, I.,Aggarwal, A.K. Structure of free BglII reveals an unprecedented scissor-like motion for opening an endonuclease. Nat.Struct.Biol., 8:126-130, 2001 Cited by PubMed Abstract: Restriction endonuclease BglII completely encircles its target DNA, making contacts to both the major and minor grooves. To allow the DNA to enter and leave the binding cleft, the enzyme dimer has to rearrange. To understand how this occurs, we have solved the structure of the free enzyme at 2.3 A resolution, as a complement to our earlier work on the BglII-DNA complex. Unexpectedly, the enzyme opens by a dramatic 'scissor-like' motion, accompanied by a complete rearrangement of the alpha-helices at the dimer interface. Moreover, within each monomer, a set of residues--a 'lever'--lowers or raises to alternately sequester or expose the active site residues. Such an extreme difference in free versus complexed structures has not been reported for other restriction endonucleases. This elegant mechanism for capturing DNA may extend to other enzymes that encircle DNA. PubMed: 11175900DOI: 10.1038/84111 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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