3MX1
The structure of GIY-YIG endonuclease R.Eco29kI
Summary for 3MX1
| Entry DOI | 10.2210/pdb3mx1/pdb |
| Related | 3MX4 |
| Descriptor | Eco29kIR (2 entities in total) |
| Functional Keywords | type ii restriction endonuclease, giy-yig endonuclease, hydrolase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 26792.99 |
| Authors | Mak, A.N.S.,Lambert, A.R.,Stoddard, B.L. (deposition date: 2010-05-06, release date: 2010-09-08, Last modification date: 2024-04-03) |
| Primary citation | Mak, A.N.,Lambert, A.R.,Stoddard, B.L. Folding, DNA Recognition, and Function of GIY-YIG Endonucleases: Crystal Structures of R.Eco29kI. Structure, 18:1321-1331, 2010 Cited by PubMed Abstract: The GIY-YIG endonuclease family comprises hundreds of diverse proteins and a multitude of functions; none have been visualized bound to DNA. The structure of the GIY-YIG restriction endonuclease R.Eco29kI has been solved both alone and bound to its target site. The protein displays a domain-swapped homodimeric structure with several extended surface loops encircling the DNA. Only three side chains from each protein subunit contact DNA bases, two directly and one via a bridging solvent molecule. Both tyrosine residues within the GIY-YIG motif are positioned in the catalytic center near a putative nucleophilic water; the remainder of the active site resembles the HNH endonuclease family. The structure illustrates how the GIY-YIG scaffold has been adapted for the highly specific recognition of a DNA restriction site, in contrast to nonspecific DNA cleavage by GIY-YIG domains in homing endonucleases or structure-specific cleavage by DNA repair enzymes such as UvrC. PubMed: 20800503DOI: 10.1016/j.str.2010.07.006 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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