6h5h | pdb_00006h5h

A computationally designed dRP lyase domain reconstructed from two heterologous fragments

spinqualitylabelsall models 6h5h Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6h5h is a 1 chain structure with sequence from Synthetic construct. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Computational design with supersecondary structures as building blocks has proven effective in the construction of new proteins with controlled geometries. So far, this approach has primarily exploited amplification, effectively harnessing the internal folding propensity of self-compatible fragments to achieve sufficient enthalpy for folding. Here we exploit an interface-driven strategy to depart from the repeat design realm, constructing an asymmetric, globular domain from heterologous supersecondary structures. We report the successful design of a dRP lyase domain fold, which agrees with the experimental NMR structure at atomic accuracy (backbone RMSD of 0.94A). Our results show that the residual folding information within conserved fragments, combined with efficient interface-directed sampling, can effectively yield globular proteins with novel sequences and biophysical properties. Asymmetric protein design from conserved supersecondary structures.,ElGamacy M, Coles M, Lupas A J Struct Biol. 2018 Dec;204(3):380-387. doi: 10.1016/j.jsb.2018.10.010. Epub 2018, Oct 26. PMID:30558718 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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