8TW0
Crystal Structure of a synthetic ABC heterotrimeric Collagen-like Peptide at 1.53 A
Summary for 8TW0
| Entry DOI | 10.2210/pdb8tw0/pdb |
| Descriptor | Collagen Mimetic Peptide A, Collagen Mimetic Peptide B, Collagen Mimetic Peptide C, ... (5 entities in total) |
| Functional Keywords | collagen mimetic peptide, triple helix, supramolecular assembly, heterotrimer, de novo design, biosynthetic protein |
| Biological source | synthetic construct More |
| Total number of polymer chains | 3 |
| Total formula weight | 9379.98 |
| Authors | Miller, M.D.,Cole, C.C.,Xu, W.,Walker, D.R.,Hulgan, S.A.H.,Pogostin, B.H.,Swain, J.W.R.,Duella, R.,Misiura, M.,Wang, X.,Kolomeisky, A.B.,Phillips Jr., G.N.,Hartgerink, J.D. (deposition date: 2023-08-18, release date: 2024-05-29, Last modification date: 2024-10-16) |
| Primary citation | Cole, C.C.,Walker, D.R.,Hulgan, S.A.H.,Pogostin, B.H.,Swain, J.W.R.,Miller, M.D.,Xu, W.,Duella, R.,Misiura, M.,Wang, X.,Kolomeisky, A.B.,Philips Jr., G.N.,Hartgerink, J.D. Heterotrimeric collagen helix with high specificity of assembly results in a rapid rate of folding. Nat.Chem., 16:1698-1704, 2024 Cited by PubMed Abstract: The most abundant natural collagens form heterotrimeric triple helices. Synthetic mimics of collagen heterotrimers have been found to fold slowly, even compared to the already slow rates of homotrimeric helices. These prolonged folding rates are not understood. Here we compare the stabilities, specificities and folding rates of three heterotrimeric collagen mimics designed through a computationally assisted approach. The crystal structure of one ABC-type heterotrimer verified a well-controlled composition and register and elucidated the geometry of pairwise cation-π and axial and lateral salt bridges in the assembly. This collagen heterotrimer folds much faster (hours versus days) than comparable, well-designed systems. Circular dichroism and NMR data suggest the folding is frustrated by unproductive, competing heterotrimer species and these species must unwind before refolding into the thermodynamically favoured assembly. The heterotrimeric collagen folding rate is inhibited by the introduction of preformed competing triple-helical assemblies, which suggests that slow heterotrimer folding kinetics are dominated by the frustration of the energy landscape caused by competing triple helices. PubMed: 39009792DOI: 10.1038/s41557-024-01573-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.53 Å) |
Structure validation
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