3IPN
Crystal Structure of fluorine and methyl modified collagen: (mepFlpgly)7
Summary for 3IPN
| Entry DOI | 10.2210/pdb3ipn/pdb |
| Descriptor | Non-natural Collagen, CARBONATE ION (3 entities in total) |
| Functional Keywords | collagen, fluorinated methylated collagen, nonnatural amino acid, structural protein |
| Total number of polymer chains | 6 |
| Total formula weight | 12246.70 |
| Authors | Satyshur, K.A.,Shoulders, M.D.,Raines, R.T.,Forest, K.T. (deposition date: 2009-08-18, release date: 2010-02-02, Last modification date: 2024-11-06) |
| Primary citation | Shoulders, M.D.,Satyshur, K.A.,Forest, K.T.,Raines, R.T. Stereoelectronic and steric effects in side chains preorganize a protein main chain. Proc.Natl.Acad.Sci.USA, 107:559-564, 2010 Cited by PubMed Abstract: Preorganization is shown to endow a protein with extraordinary conformational stability. This preorganization is achieved by installing side-chain substituents that impose stereoelectronic and steric effects that restrict main-chain torsion angles. Replacing proline residues in (ProProGly)(7) collagen strands with 4-fluoroproline and 4-methylproline leads to the most stable known triple helices, having T ( m ) values that are increased by > 50 degrees C. Differential scanning calorimetry data indicate an entropic basis to the hyperstability, as expected from an origin in preorganization. Structural data at a resolution of 1.21 A reveal a prototypical triple helix with insignificant deviations to its main chain, even though 2/3 of the residues are nonnatural. Thus, preorganization of a main chain by subtle changes to side chains can confer extraordinary conformational stability upon a protein without perturbing its structure. PubMed: 20080719DOI: 10.1073/pnas.0909592107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.21 Å) |
Structure validation
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