Abstract
We have solved the structure of a chimeric T7/T3 RNA polymerase (RNAP) in an orthorhombic crystal by molecular replacement with the T7 RNAP structure determined from a monoclinic crystal. The structure of the protruding "thumb" subdomain of the polymerase appears very different in these two crystals apparently because of differences in packing contacts made by the thumb subdomain. These observations support the proposal that the thumb subdomain is flexible and can wrap around bound template to obstruct polymerase : template dissociation during processive synthesis.
Original language | English (US) |
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Pages (from-to) | 6-12 |
Number of pages | 7 |
Journal | Journal of Molecular Biology |
Volume | 244 |
Issue number | 1 |
DOIs | |
State | Published - 1994 |
Keywords
- Molecular replacement
- Polymerase
- Processivity
- Protein flexibility
- RNA polymerase
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology