5o94 | pdb_00005o94

X-ray structure of a zinc binding GB1 mutant

spinqualitylabelsall models 5o94, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5o94 is a 1 chain structure with sequence from Streptococcus sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: EDO, GOL, MPD, NA, SO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The development of thermostable and solvent-tolerant metalloproteins is a long-sought goal for many applications in synthetic biology and biotechnology. In this work, we were able to engineer a highly thermostable and organic solvent-stable metallo variant of the B1 domain of protein G (GB1) with a tetrahedral zinc binding site reminiscent of the one of thermolysin. Promising candidates were designed computationally by applying a protocol based on classical and first-principles molecular dynamics simulations in combination with genetic algorithm optimization. The most promising of the computationally predicted mutants was expressed and structurally characterized and yielded a highly thermostable protein. The experimental results thus confirm the predictive power of the applied computational protein engineering approach for the de novo design of highly stable metalloproteins. Genetic Algorithm Based Design and Experimental Characterization of a Highly Thermostable Metalloprotein.,Bozkurt E, Perez MAS, Hovius R, Browning NJ, Rothlisberger U J Am Chem Soc. 2018 Mar 26. doi: 10.1021/jacs.7b10660. PMID:29336153 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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