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Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae
Published on: January 10, 2018
Nucleotide-bound crystal structures of the SARS-CoV-2 helicase NSP13
Patrick Kloskowski1, Piotr Neumann1, Annette Berndt1
1Department of Molecular Structural Biology, Institute of Microbiology and Genetics, Göttingen Center of Molecular Biosciences (GZMB), University of Göttingen, Justus-von-Liebig-Weg 11, 37077 Göttingen, Germany.
None:
Nucleotide-bound crystal structures of SARS-CoV-2 NSP13 in ADP- and ATP-bound states were resolved to 1.8 and 1.9 Å, respectively. The ADP-bound model captures a state immediately following ATP hydrolysis, with both ADP and orthophosphate still present in the active site. Further comparative analysis revealed that crystal packing influences NSP13 by stabilizing the nucleotide-binding site, underscoring the importance of accounting for these effects in structure-based drug design targeting NSP13.
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