This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. We are investigating the structures of catalytic RNAs (or ribozymes) and RNAs derived from viruses. We have obtained new crystal structures during the last beamtime allocation period of a highly conserved region of the SARS virus RNA genome called the s2m RNA, thought to be critical to the life-cycle of this pathogenic virus, a new structure of the hammerhead ribozyme (originally discovered in the context of various plant satellite RNA viruses), and a new structure of an in vitro evolved RNA ligase that catalyzes a reaction thought to be of critical importance for the evolution of RNA selfreplication in a prebiotic RNA world. We propose to continue structural investigations of all three RNA systems during the next beamtime allocation period. Specifically, cocrystals of the SARS s2m RNA bound to peptides and small molecules, as well as SARS RNA/protein complex structures, will be solved, catalytic variants and mutants of the new hammerhead ribozyme structure will be analyzed, and a pre-ligation state of the in vitro evolved RNA ligase will be obtained.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR001209-31
Application #
8169930
Study Section
Special Emphasis Panel (ZRG1-BCMB-P (40))
Project Start
2010-05-01
Project End
2011-02-28
Budget Start
2010-05-01
Budget End
2011-02-28
Support Year
31
Fiscal Year
2010
Total Cost
$2,040
Indirect Cost
Name
Stanford University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
009214214
City
Stanford
State
CA
Country
United States
Zip Code
94305
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Herrera, Nadia; Maksaev, Grigory; Haswell, Elizabeth S et al. (2018) Elucidating a role for the cytoplasmic domain in the Mycobacterium tuberculosis mechanosensitive channel of large conductance. Sci Rep 8:14566
Dods, Robert; Båth, Petra; Arnlund, David et al. (2017) From Macrocrystals to Microcrystals: A Strategy for Membrane Protein Serial Crystallography. Structure 25:1461-1468.e2
de Vries, Robert P; Tzarum, Netanel; Peng, Wenjie et al. (2017) A single mutation in Taiwanese H6N1 influenza hemagglutinin switches binding to human-type receptors. EMBO Mol Med 9:1314-1325

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