2G7H
Structure of an O6-Methylguanine DNA Methyltransferase from Methanococcus jannaschii (MJ1529)
Summary for 2G7H
| Entry DOI | 10.2210/pdb2g7h/pdb |
| NMR Information | BMRB: 7122 |
| Descriptor | Methylated-DNA--protein-cysteine methyltransferase (1 entity in total) |
| Functional Keywords | protein structure, dna repair, dna methyltransferase, transferase |
| Biological source | Methanocaldococcus jannaschii |
| Cellular location | Cytoplasm (By similarity): Q58924 |
| Total number of polymer chains | 1 |
| Total formula weight | 19460.94 |
| Authors | Roberts, A. (deposition date: 2006-02-28, release date: 2006-08-01, Last modification date: 2024-05-29) |
| Primary citation | Roberts, A.,Pelton, J.G.,Wemmer, D.E. Structural studies of MJ1529, an O(6)-methylguanine-DNA methyltransferase Magn.Reson.Chem., 44:71-82, 2006 Cited by PubMed Abstract: The structure of an O6-methylguanine-DNA methyltransferase (MGMT) from the thermophile Methanococcus jannaschii has been determined using multinuclear multidimensional NMR spectroscopy. The structure is similar to homologs from other organisms that have been determined by crystallography, with some variation in the N-terminal domain. The C-terminal domain is more highly conserved in both sequence and structure. Regions of the protein show broadening, reflecting conformational flexibility that is likely related to function. PubMed: 16826543DOI: 10.1002/mrc.1823 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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