6Q8V
Structure of the standard kink turn HmKt-7 variant A2bm6A.
Summary for 6Q8V
| Entry DOI | 10.2210/pdb6q8v/pdb |
| Descriptor | RNA (5'-R(*GP*GP*CP*GP*AP*AP*GP*(6MZ)P*AP*CP*CP*GP*GP*GP*GP*AP*GP*CP*C)-3') (2 entities in total) |
| Functional Keywords | gene regulation; rna structure; kink-turn; x-ray crystallography; rna modification, rna |
| Biological source | Haloarcula marismortui |
| Total number of polymer chains | 1 |
| Total formula weight | 6247.86 |
| Authors | Huang, L.,Lilley, D.M.J. (deposition date: 2018-12-16, release date: 2019-07-03, Last modification date: 2024-01-24) |
| Primary citation | Ashraf, S.,Huang, L.,Lilley, D.M.J. Effect of methylation of adenine N6on kink turn structure depends on location. Rna Biol., 16:1377-1385, 2019 Cited by PubMed Abstract: N-methyladenine is the most common covalent modification in cellular RNA species, with demonstrated functional consequences. At the molecular level this methylation could alter local RNA structure, and/or modulate the binding of specific proteins. We have previously shown that -Hoogsteen-sugar (sheared) A:G base pairs can be completely disrupted by methylation, and that this occurs in a sub-set ofD/D k-turn structures. In this work we have investigated to what extent sequence context affects the severity with which inclusion of N-methyladenine into different A:G base pairs of a standard k-turn affects RNA folding and L7Ae protein binding. We find that local sequence has a major influence, ranging from complete absence of folding and protein binding to a relatively mild effect. We have determined the crystal structure of one of these species both free and protein-bound, showing the environment of the methyl group and the way the modification is accommodated into the k-turn structure. PubMed: 31234702DOI: 10.1080/15476286.2019.1630797 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.09 Å) |
Structure validation
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