2013年10月
Crystal structure at 1.5 angstrom resolution of the PsbV2 cytochrome from the cyanobacterium Thermosynechococcus elongatus
FEBS LETTERS
- ,
- ,
- ,
- ,
- 巻
- 587
- 号
- 19
- 開始ページ
- 3267
- 終了ページ
- 3272
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.febslet.2013.08.023
- 出版者・発行元
- WILEY
PsbV2 is a c-type cytochrome present in a very low abundance in the thermophilic cyanobacterium Thermosynechococcus elongatus. We purified this cytochrome and solved its crystal structure at a resolution of 1.5 angstrom. The protein existed as a dimer in the crystal, and has an overall structure similar to other c-type cytochromes like Cytc(6) and Cytc(550), for example. However, the 5th and 6th heme iron axial ligands were found to be His51 and Cys101, respectively, in contrast to the more common bis-His or His/Met ligands found in most cytochromes. Although a few other c-type cytochromes were suggested to have this axial coordination, this is the first crystal structure reported for a c-type heme with this unusual His/Cys axial coordination. Previous spectroscopic characterizations of PsbV2 are discussed in relation to its structural properties. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
- リンク情報
- ID情報
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- DOI : 10.1016/j.febslet.2013.08.023
- ISSN : 0014-5793
- eISSN : 1873-3468
- PubMed ID : 23994160
- Web of Science ID : WOS:000324472200017