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Structure and mobility of the PUT3 dimer
K J Walters1, K T Dayie, R J Reece
1Committee on Higher Degrees in Biophysics, Harvard University, Cambridge, Massachusetts 02138, USA.
Nature Structural Biology
|September 26, 1997
Summary
The transcriptional activator PUT3 (31-100) protein
Area of Science:
- Molecular biology
- Structural biology
- Biochemistry
Background:
- PUT3 is a transcriptional activator involved in gene regulation.
- PUT3 (31-100) comprises three domains: a cysteine zinc cluster, linker, and dimerization domain.
Purpose of the Study:
- To characterize the solution structure and backbone dynamics of PUT3 (31-100).
- To compare PUT3's structural features with related proteins like GAL4 and PPR1.
- To develop a model for DNA binding specificity based on structural comparisons.
Main Methods:
- Nuclear Magnetic Resonance (NMR) spectroscopy was employed to determine the solution structure.
- Backbone dynamics were analyzed using NMR data.
- Structural comparisons were made with existing crystal structures of GAL4 and PPR1.
Main Results:
- The cysteine zinc cluster of PUT3 resembles GAL4's structure.
- The dimerization domain forms a coiled-coil similar to GAL4 and PPR1, but with distinct N-terminal dynamics.
- PUT3 exhibits diverse dynamics between its zinc cluster and dimerization domains.
Conclusions:
- Structural similarities and differences provide insights into DNA binding specificity.
- The distinct dynamics of PUT3's domains suggest functional specialization.
- PUT3's zinc clusters show dynamics akin to small proteins, while the dimerization domain behaves like a large protein.