We have been studying E. coli DNA topoisomerase I and III for a number of years and have proposed a catalytic mechanism. We are studying the interactions of topoisomerase I with DNA and also the structure of mutant proteins that could shed light on the details of the reaction. We solved the structure of two repeats of chicken brain ?-spectrin in 1997 using data collected at SSRL. The structure revealed the relative arrangement of the two subunits and the nature of the linker region. The original crystals diffract to only 4.0 E resolution and many questions could not be answered from this structure. Nevertheless the structure allowed us to redesign our construct and obtain better crystals. We have now three new crystal forms that diffract to high resolution. The third project is concerned with the structure of domain I of the RNA component of RNase P. This domain is 154 bases long and the crystals diffract to 3.8 E at a synchrotron source. It is one of the largest RNA molecules crystallized and should allow us to answer important questions on the catalytic mechanism of RNase P and also on RNA structure in general.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001209-20
Application #
6119376
Study Section
Project Start
1999-03-01
Project End
2000-04-14
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
20
Fiscal Year
1999
Total Cost
Indirect Cost
Name
Stanford University
Department
Type
DUNS #
800771545
City
Stanford
State
CA
Country
United States
Zip Code
94305
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Hettle, Andrew; Fillo, Alexander; Abe, Kento et al. (2017) Properties of a family 56 carbohydrate-binding module and its role in the recognition and hydrolysis of ?-1,3-glucan. J Biol Chem 292:16955-16968
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