Abstract
The three-dimensional structure of bacteriophage φX174 external scaffolding protein D, prior to its interaction with other structural proteins, has been determined to 3.3 Å by X-ray crystallography. The crystals belong to space group P41212 with a dimer in the asymmetric unit that closely resembles asymmetric dimers observed in the φX174 procapsid structure. Furthermore, application of the crystallographic 41 symmetry operation to one of these dimers generates a tetramer similar to the tetramer in the icosahedral asymmetric unit of the procapsid. These data suggest that both dimers and tetramers of the D protein are true morphogenetic intermediates and can form independently of other proteins involved in procapsid morphogenesis. The crystal structure of the D scaffolding protein thus represents the state of the polypeptide prior to procapsid assembly. Hence, comparison with the procapsid structure provides a rare opportunity to follow the conformational switching events necessary for the construction of complex macromolecular assemblies.
| Original language | English |
|---|---|
| Pages (from-to) | 991-997 |
| Number of pages | 7 |
| Journal | Molecular Cell |
| Volume | 15 |
| Issue number | 6 |
| DOIs | |
| State | Published - Sep 24 2004 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Molecular Biology
Cite this
Conformational switching by the scaffolding protein D directs the assembly of bacteriophage φX174. / Morais, Marc; Fisher, Megan; Kanamaru, Shuji; Przybyla, Laralynne; Burgner, John; Fane, Bentley A.; Rossmann, Michael G.
In: Molecular Cell, Vol. 15, No. 6, 24.09.2004, p. 991-997.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Conformational switching by the scaffolding protein D directs the assembly of bacteriophage φX174
AU - Morais, Marc
AU - Fisher, Megan
AU - Kanamaru, Shuji
AU - Przybyla, Laralynne
AU - Burgner, John
AU - Fane, Bentley A.
AU - Rossmann, Michael G.
PY - 2004/9/24
Y1 - 2004/9/24
N2 - The three-dimensional structure of bacteriophage φX174 external scaffolding protein D, prior to its interaction with other structural proteins, has been determined to 3.3 Å by X-ray crystallography. The crystals belong to space group P41212 with a dimer in the asymmetric unit that closely resembles asymmetric dimers observed in the φX174 procapsid structure. Furthermore, application of the crystallographic 41 symmetry operation to one of these dimers generates a tetramer similar to the tetramer in the icosahedral asymmetric unit of the procapsid. These data suggest that both dimers and tetramers of the D protein are true morphogenetic intermediates and can form independently of other proteins involved in procapsid morphogenesis. The crystal structure of the D scaffolding protein thus represents the state of the polypeptide prior to procapsid assembly. Hence, comparison with the procapsid structure provides a rare opportunity to follow the conformational switching events necessary for the construction of complex macromolecular assemblies.
AB - The three-dimensional structure of bacteriophage φX174 external scaffolding protein D, prior to its interaction with other structural proteins, has been determined to 3.3 Å by X-ray crystallography. The crystals belong to space group P41212 with a dimer in the asymmetric unit that closely resembles asymmetric dimers observed in the φX174 procapsid structure. Furthermore, application of the crystallographic 41 symmetry operation to one of these dimers generates a tetramer similar to the tetramer in the icosahedral asymmetric unit of the procapsid. These data suggest that both dimers and tetramers of the D protein are true morphogenetic intermediates and can form independently of other proteins involved in procapsid morphogenesis. The crystal structure of the D scaffolding protein thus represents the state of the polypeptide prior to procapsid assembly. Hence, comparison with the procapsid structure provides a rare opportunity to follow the conformational switching events necessary for the construction of complex macromolecular assemblies.
UR - http://www.scopus.com/inward/record.url?scp=4644230086&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=4644230086&partnerID=8YFLogxK
U2 - 10.1016/j.molcel.2004.08.023
DO - 10.1016/j.molcel.2004.08.023
M3 - Article
C2 - 15383287
AN - SCOPUS:4644230086
VL - 15
SP - 991
EP - 997
JO - Molecular Cell
JF - Molecular Cell
SN - 1097-2765
IS - 6
ER -