Journal Article PUBDB-2025-04027

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Nucleotide-bound crystal structures of the SARS-CoV-2 helicase NSP13

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2025
Blackwell Oxford [u.a.]

Acta crystallographica / Section F 81(8), 338 - 347 () [10.1107/S2053230X25005266]
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Abstract: 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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Note: Funding for this research was provided by the DeutscheForschungsgemeinschaft (Germany’s Excellence StrategyEXC 2067/1-390729940 to RF and grant No. INST186/1117 toRF).

Contributing Institute(s):
  1. EMBL-User (EMBL-User)
Research Program(s):
  1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)
  2. DFG project G:(GEPRIS)390729940 - EXC 2067: Multiscale Bioimaging: Von molekularen Maschinen zu Netzwerken erregbarer Zellen (390729940) (390729940)
Experiment(s):
  1. PETRA Beamline P13 (PETRA III)

Appears in the scientific report 2025
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Medline ; Creative Commons Attribution CC BY 4.0 ; OpenAccess ; BIOSIS Previews ; Biological Abstracts ; Clarivate Analytics Master Journal List ; DEAL Wiley ; Ebsco Academic Search ; Essential Science Indicators ; IF < 5 ; JCR ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection
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 Record created 2025-09-19, last modified 2025-11-19


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