Structure and dynamics of the N-terminal loop of PsbQ from photosystem II of Spinacia oleracea
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.
PubMed
16678136
DOI
10.1016/j.bbrc.2006.04.087
PII: S0006-291X(06)00885-0
Knihovny.cz E-resources
- MeSH
- Models, Chemical * MeSH
- Photosynthetic Reaction Center Complex Proteins analysis chemistry ultrastructure MeSH
- Photosystem II Protein Complex analysis chemistry ultrastructure MeSH
- Protein Conformation MeSH
- Models, Molecular * MeSH
- Molecular Sequence Data MeSH
- Computer Simulation MeSH
- Plant Proteins analysis chemistry ultrastructure MeSH
- Protein Structure, Secondary MeSH
- Amino Acid Sequence MeSH
- Spinacia oleracea chemistry MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
- Names of Substances
- Photosynthetic Reaction Center Complex Proteins MeSH
- Photosystem II Protein Complex MeSH
- Plant Proteins MeSH
Infrared and Raman spectroscopy were applied to identify restraints for the structure determination of the 20 amino acid loop between two beta-sheets of the N-terminal region of the PsbQ protein of the oxygen evolving complex of photosystem II from Spinacia oleracea by restraint-based homology modeling. One of the initial models has shown a stable fold of the loop in a 20 ns molecular dynamics simulation that is in accordance with spectroscopic data. Cleavage of the first 12 amino acids leads to a permanent drift in the root means square deviation of the protein backbone and induces major structural changes.
Biochem Biophys Res Commun. 2006 Sep 29;348(3):1205 PubMed
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