7DXR
Crystal structure of the mk2h peptide homodimer.
Summary for 7DXR
| Entry DOI | 10.2210/pdb7dxr/pdb |
| Descriptor | mk2h protein, SULFATE ION, 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID, ... (4 entities in total) |
| Functional Keywords | double psi beta barrel, chaperone |
| Biological source | synthetic construct |
| Total number of polymer chains | 4 |
| Total formula weight | 21854.40 |
| Authors | Yagi, S.,Tagami, S. (deposition date: 2021-01-20, release date: 2021-09-29, Last modification date: 2023-11-29) |
| Primary citation | Yagi, S.,Padhi, A.K.,Vucinic, J.,Barbe, S.,Schiex, T.,Nakagawa, R.,Simoncini, D.,Zhang, K.Y.J.,Tagami, S. Seven Amino Acid Types Suffice to Create the Core Fold of RNA Polymerase. J.Am.Chem.Soc., 143:15998-16006, 2021 Cited by PubMed Abstract: The extant complex proteins must have evolved from ancient short and simple ancestors. The double-ψ β-barrel (DPBB) is one of the oldest protein folds and conserved in various fundamental enzymes, such as the core domain of RNA polymerase. Here, by reverse engineering a modern DPBB domain, we reconstructed its plausible evolutionary pathway started by "interlacing homodimerization" of a half-size peptide, followed by gene duplication and fusion. Furthermore, by simplifying the amino acid repertoire of the peptide, we successfully created the DPBB fold with only seven amino acid types (Ala, Asp, Glu, Gly, Lys, Arg, and Val), which can be coded by only GNN and ARR (R = A or G) codons in the modern translation system. Thus, the DPBB fold could have been materialized by the early translation system and genetic code. PubMed: 34559526DOI: 10.1021/jacs.1c05367 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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