The cyanobacterial cytochrome b6f subunit PetP adopts an SH3 fold in solution
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- 作者：Sebastian Veita ; Aritaka Nagadoic ; Matthias Rö ; gnera ; Sascha Rexrotha ; sascha.rexroth@ruhr-uni-bochum.de" class="auth_mail" title="E-mail the corresponding author ; Raphael Stollb ; raphael.stoll@ruhr-uni-bochum.de" class="auth_mail" title="E-mail the corresponding author ; Takahisa Ikegamic ; 1 ; ikegamit@yokohama-cu.ac.jp" class="auth_mail" title="E-mail the corresponding author
- 关键词：b6f ; cytochrome b6f complex ; PS1 ; photosystem 1 ; PS2 ; photosystem 2 ; NDH-1 ; NADH dehydrogenase-like complex ; FTR ; ferredoxin&ndash ; thioredoxin reductase ; Fd ; ferredoxin ; PC ; plastocyanin ; Cyt. c6 ; cytochrome c6 ; FNR ; ferredoxin-NADP+ reductase ; PQ ; plastoquinone ; LET ; linear electron transport ; CET ; cyclic electron transport ; SH3 domain ; Src-homology 3 domain ; NMR ; nuclear magnetic resonance spectroscopy ; NOE ; nuclear overhauser effect ; RCI ; random coil index
- 刊名：Biochimica et Biophysica Acta (BBA) - Bioenergetics
- 出版年：2016
- 出版时间：June 2016
- 年：2016
- 卷：1857
- 期：6
- 页码：705-714
- 全文大小：1536 K
文摘
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Solution structure of the cyanobacterial cyt. b6f subunit PetP has been determined.
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PetP adopts an SH3 domain fold similar to subunits of PS1, NDH-1 and FTR.
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Heteronuclear steady-state {1H}–15N NOE and RCI parameters have been determined.
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The potential interaction surface for b6f binding is described.
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A model of the roles of SH3 domains in oxygenic photosynthesis is presented.