2HMY
BINARY COMPLEX OF HHAI METHYLTRANSFERASE WITH ADOMET FORMED IN THE PRESENCE OF A SHORT NONPSECIFIC DNA OLIGONUCLEOTIDE
Summary for 2HMY
| Entry DOI | 10.2210/pdb2hmy/pdb |
| Descriptor | PROTEIN (CYTOSINE-SPECIFIC METHYLTRANSFERASE HHAI), S-ADENOSYLMETHIONINE (3 entities in total) |
| Functional Keywords | transferase (methyltransferase) |
| Biological source | Haemophilus haemolyticus |
| Total number of polymer chains | 1 |
| Total formula weight | 37440.64 |
| Authors | O'Gara, M.,Zhang, X.,Roberts, R.J.,Cheng, X. (deposition date: 1999-02-08, release date: 1999-03-19, Last modification date: 2023-08-30) |
| Primary citation | O'Gara, M.,Zhang, X.,Roberts, R.J.,Cheng, X. Structure of a binary complex of HhaI methyltransferase with S-adenosyl-L-methionine formed in the presence of a short non-specific DNA oligonucleotide. J.Mol.Biol., 287:201-209, 1999 Cited by PubMed Abstract: We have determined a structure for a complex formed between HhaI methyltransferase (M.HhaI) and S-adenosyl-L-methionine (AdoMet) in the presence of a non-specific short oligonucleotide. M.HhaI binds to the non-specific short oligonucleotides in solution. Although no DNA is incorporated in the crystal, AdoMet binds in a primed orientation, identical with that observed in the ternary complex of the enzyme, cognate DNA, and AdoMet or S-adenosyl-L-homocysteine (AdoHcy). This orientation differs from the previously observed unprimed orientation in the M.HhaI-AdoMet binary complex, where the S+-CH3 unit of AdoMet is protected by a favorable cation-pi interaction with Trp41. The structure suggests that the presence of DNA can guide AdoMet into the primed orientation. These results shed new light on the proposed ordered mechanism of binding and explains the stable association between AdoMet and M.HhaI. PubMed: 10080885DOI: 10.1006/jmbi.1999.2608 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.61 Å) |
Structure validation
Download full validation report
