6VGB
De novo designed Rossmann fold protein ROS2_36830
Summary for 6VGB
| Entry DOI | 10.2210/pdb6vgb/pdb |
| NMR Information | BMRB: 30708 |
| Descriptor | De novo designed protein RO2_20 (1 entity in total) |
| Functional Keywords | rossmann fold, de novo protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 13953.31 |
| Authors | Pan, X.,Zhang, Y.,Kelly, M.,Kortemme, T. (deposition date: 2020-01-07, release date: 2020-08-19, Last modification date: 2024-05-15) |
| Primary citation | Pan, X.,Thompson, M.C.,Zhang, Y.,Liu, L.,Fraser, J.S.,Kelly, M.J.S.,Kortemme, T. Expanding the space of protein geometries by computational design of de novo fold families. Science, 369:1132-1136, 2020 Cited by PubMed Abstract: Naturally occurring proteins vary the precise geometries of structural elements to create distinct shapes optimal for function. We present a computational design method, loop-helix-loop unit combinatorial sampling (LUCS), that mimics nature's ability to create families of proteins with the same overall fold but precisely tunable geometries. Through near-exhaustive sampling of loop-helix-loop elements, LUCS generates highly diverse geometries encompassing those found in nature but also surpassing known structure space. Biophysical characterization showed that 17 (38%) of 45 tested LUCS designs encompassing two different structural topologies were well folded, including 16 with designed non-native geometries. Four experimentally solved structures closely matched the designs. LUCS greatly expands the designable structure space and offers a new paradigm for designing proteins with tunable geometries that may be customizable for novel functions. PubMed: 32855341DOI: 10.1126/science.abc0881 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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