2LZE
Ligase 10C
Summary for 2LZE
| Entry DOI | 10.2210/pdb2lze/pdb |
| NMR Information | BMRB: 18749 |
| Descriptor | a primordial catalytic fold generated by in vitro evolution, ZINC ION (2 entities in total) |
| Functional Keywords | ligase, de novo protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 9926.70 |
| Authors | Chao, F.,Morelli, A.,Haugner, J.,Churchfield, L.,Hagmann, L.,Shi, L.,Masterson, L.,Sarangi, R.,Veglia, G.,Seelig, B. (deposition date: 2012-10-01, release date: 2012-10-24, Last modification date: 2024-05-01) |
| Primary citation | Chao, F.A.,Morelli, A.,Iii, J.C.,Churchfield, L.,Hagmann, L.N.,Shi, L.,Masterson, L.R.,Sarangi, R.,Veglia, G.,Seelig, B. Structure and dynamics of a primordial catalytic fold generated by in vitro evolution. Nat.Chem.Biol., 9:81-83, 2013 Cited by PubMed Abstract: Engineering functional protein scaffolds capable of carrying out chemical catalysis is a major challenge in enzyme design. Starting from a noncatalytic protein scaffold, we recently generated a new RNA ligase by in vitro directed evolution. This artificial enzyme lost its original fold and adopted an entirely new structure with substantially enhanced conformational dynamics, demonstrating that a primordial fold with suitable flexibility is sufficient to carry out enzymatic function. PubMed: 23222886DOI: 10.1038/nchembio.1138 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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