Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10795336 | Biochimica et Biophysica Acta (BBA) - Bioenergetics | 2015 | 8 Pages |
Abstract
Here, we present the NMR structure of CupS from Thermosynechococcus elongatus, which is the very first structure of a specific cyanobacterial NDH-1 complex subunit. CupS shares a structural similarity with members of the Fasciclin protein superfamily. The structural comparison to Fasciclin type proteins based on known NMR structures and protein sequences of human TGFBIp, MPB70 from Mycobacterium bovis, and Fdp from Rhodobacter sphaeroides, together with a virtual docking model of CupS and NdhF3, provide first insight into the specific binding of CupS to the NDH-1MS complex at atomic resolution.
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Authors
Annika Korste, Hannes Wulfhorst, Takahisa Ikegami, Marc M. Nowaczyk, Raphael Stoll,