1qys

Crystal structure of Top7: A computationally designed protein with a novel fold

spinqualitylabelsall models 1qys, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1qys is a 1 chain structure with sequence from Computationally Designed Sequence. The October 2005 RCSB PDB Molecule of the Month feature on Designer Proteins by David S. Goodsell is 10.2210/rcsb_pdb/mom_2005_10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed A major challenge of computational protein design is the creation of novel proteins with arbitrarily chosen three-dimensional structures. Here, we used a general computational strategy that iterates between sequence design and structure prediction to design a 93-residue alpha/beta protein called Top7 with a novel sequence and topology. Top7 was found experimentally to be folded and extremely stable, and the x-ray crystal structure of Top7 is similar (root mean square deviation equals 1.2 angstroms) to the design model. The ability to design a new protein fold makes possible the exploration of the large regions of the protein universe not yet observed in nature. Design of a novel globular protein fold with atomic-level accuracy.,Kuhlman B, Dantas G, Ireton GC, Varani G, Stoddard BL, Baker D Science. 2003 Nov 21;302(5649):1364-8. PMID:14631033 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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