NOE distance and dihedral angle restraints to calculate the solution structure of the NDH-1 complex subunit CupS from Thermosynechococcus elongatus

• Published in: Data in brief 2016-03, Vol.6, p.249-252
• Main Authors: Korste, Annika, Wulfhorst, Hannes, Ikegami, Takahisa, Nowaczyk, Marc M., Stoll, Raphael
• Format: Article
• Language: English
• Subjects: Bioenergetics/electron Transfer Complex; CupS; Cyanobacteria; Data; Membrane Proteins; NMR Protein Structure; NOE Distance And Dihedral Angle Restraints
• ISSN: 2352-3409; 2352-3409
• DOI: 10.1016/j.dib.2015.12.004

Here, we have compiled a nuclear magnetic resonance (NMR)-derived set of nuclear Overhauser enhancement (NOE) distance and dihedral angle restraints that allow for the calculation of the structure of the NDH-1 complex subunit CupS from Thermosynechococcus elongatus in solution. These restraints to calculate the structure in solution of CupS have been deposited to the Protein Data Bank (www.rcsb.org) under PDB-ID accession number 2MXA. This is the first experimental data set published to compute the three-dimensional structure of CupS. This structure is presented in the research article “Solution structure of the NDH-1 complex subunit CupS from Thermosynechococcus elongatus” published by Korste et al. in Biochim. Biophys. Acta 1847(2015)1212–1219 [1]. The cyanobacterial multi-subunit membrane protein complex NDH-1 structurally and functionally relates to Complex I of eubacteria and mitochondria. The NDH-1 complex is mechanistically involved in respiration and cyclic electron transfer around photosystem I (PSI) as well as in a unique mechanism for inorganic carbon concentration.