4CS1
Crystal structure of a simple duplex kink turn, HmKt-7 with 2 Mg bound.
Summary for 4CS1
| Entry DOI | 10.2210/pdb4cs1/pdb |
| Descriptor | 5'-(*GP*GP*CP*GP*AP*AP*GP*AP*AP*CP*CP*GP*GP*GP *GP*AP*GP*CP*CP)-3', MAGNESIUM ION (3 entities in total) |
| Functional Keywords | rna, kink turn, metal ion |
| Biological source | HALOARCULA MARISMORTUI |
| Total number of polymer chains | 1 |
| Total formula weight | 6282.44 |
| Authors | Huang, L.,Lilley, D.M.J. (deposition date: 2014-03-03, release date: 2014-11-19, Last modification date: 2023-12-20) |
| Primary citation | Mcphee, S.A.,Huang, L.,Lilley, D.M.J. A Critical Base Pair in K-Turns that Confers Folding Characteristics and Correlates with Biological Function. Nat.Commun., 5:5127-, 2014 Cited by PubMed Abstract: Kink turns (k-turns) are widespread elements in RNA that mediate tertiary contacts by kinking the helical axis. We have found that the ability of k-turns to undergo ion-induced folding is conferred by a single base pair that follows the conserved A·G pairs, that is, the 3b·3n position. A Watson-Crick pair leads to an inability to fold in metal ions alone, while 3n=G or 3b=C (but not both) permits folding. Crystallographic study reveals two hydrated metal ions coordinated to O6 of G3n and G2n of Kt-7. Removal of either atom impairs Mg(2+)-induced folding in solution. While SAM-I riboswitches have 3b·3n sequences that would predispose them to ion-induced folding, U4 snRNA are strongly biased to an inability to such folding. Thus riboswitch sequences allow folding to occur independently of protein binding, while U4 should remain unfolded until bound by protein. The empirical rules deduced for k-turn folding have strong predictive value. PubMed: 25351101DOI: 10.1038/NCOMMS6127 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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