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) |
|---|---|
| Pages (from-to) | 6-12 |
| Number of pages | 7 |
| Journal | Journal of Molecular Biology |
| Volume | 244 |
| Issue number | 1 |
| State | Published - 1994 |
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Keywords
- Molecular replacement
- Polymerase
- Processivity
- Protein flexibility
- RNA polymerase
ASJC Scopus subject areas
- Virology
Cite this
The thumb's knuckle : Flexibility in the thumb subdomain of T7 RNA polymerase is revealed by the structure of a chimeric T7/T3 RNA polymerase. / Sousa, Rui J; Rose, John; Wang, B. C.
In: Journal of Molecular Biology, Vol. 244, No. 1, 1994, p. 6-12.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The thumb's knuckle
T2 - Flexibility in the thumb subdomain of T7 RNA polymerase is revealed by the structure of a chimeric T7/T3 RNA polymerase
AU - Sousa, Rui J
AU - Rose, John
AU - Wang, B. C.
PY - 1994
Y1 - 1994
N2 - 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.
AB - 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.
KW - Molecular replacement
KW - Polymerase
KW - Processivity
KW - Protein flexibility
KW - RNA polymerase
UR - http://www.scopus.com/inward/record.url?scp=0028035156&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028035156&partnerID=8YFLogxK
M3 - Article
C2 - 7966322
AN - SCOPUS:0028035156
VL - 244
SP - 6
EP - 12
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 1
ER -