8QXI
SipA solution structure
Summary for 8QXI
| Entry DOI | 10.2210/pdb8qxi/pdb |
| NMR Information | BMRB: 52171 |
| Descriptor | Uncharacterized protein SEF0032 (1 entity in total) |
| Functional Keywords | interacting nbls protein, cyanobacteria, unknown function |
| Biological source | Synechocystis |
| Total number of polymer chains | 1 |
| Total formula weight | 8515.67 |
| Authors | |
| Primary citation | Neira, J.L.,Lopez-Redondo, M.L.,Camara-Artigas, A.,Marina, A.,Contreras, A. Structure and dynamics of the cyanobacterial regulator SipA. Arch.Biochem.Biophys., 754:109943-109943, 2024 Cited by PubMed Abstract: The small, 78-residue long, regulator SipA interacts with the non-bleaching sensor histidine kinase (NblS). We have solved the solution structure of SipA on the basis of 990 nuclear Overhauser effect- (NOE-) derived distance constraints. The average pairwise root-mean-square deviation (RMSD) for the twenty best structures for the backbone residues, obtained by CYANA, was 1.35 ± 0.21 Å, and 1.90 ± 0.16 Å when all heavy atoms were considered (the target function of CYANA was 0.540 ± 0.08). The structure is that of a β-II class protein, basically formed by a five-stranded β-sheet composed of antiparallel strands following the arrangement: Gly6-Leu11 (β-strand 1), which packs against Leu66-Val69 (β-strand 5) on one side, and against Gly36-Thr42 (β-strand 2) on the other side; Trp50-Phe54 (β-strand 3); and Gly57-Leu60 (β-strand 4). The protein is highly mobile, as shown by measurements of R, R, NOE and η relaxation parameters, with an average order parameter ( DOI: 10.1016/j.abb.2024.109943 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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