2K6I
The domain features of the peripheral stalk subunit H of the methanogenic A1AO ATP synthase and the NMR solution structure of H1-47
Summary for 2K6I
| Entry DOI | 10.2210/pdb2k6i/pdb |
| NMR Information | BMRB: 15870 |
| Descriptor | Uncharacterized protein MJ0223 (1 entity in total) |
| Functional Keywords | h subunit, a1ao atp synthase, v1vo atpase, f1fo atp synthase, methanocaldococcus jannaschii, structural protein |
| Biological source | Methanocaldococcus jannaschii (Methanococcus jannaschii) |
| Total number of polymer chains | 1 |
| Total formula weight | 6394.44 |
| Authors | Biukovic, N.,Gayen, S.,Pervushin, K.,Gruber, G.,Biukovic, G. (deposition date: 2008-07-09, release date: 2009-07-21, Last modification date: 2024-05-08) |
| Primary citation | Biukovic, G.,Gayen, S.,Pervushin, K.,Gruber, G. Domain features of the peripheral stalk subunit H of the methanogenic A1AO ATP synthase and the NMR solution structure of H(1-47). Biophys.J., 97:286-294, 2009 Cited by PubMed Abstract: A series of truncated forms of subunit H were generated to establish the domain features of that protein. Circular dichroism analysis demonstrated that H is divided at least into a C-terminal coiled-coil domain within residues 54-104, and an N-terminal domain formed by adjacent alpha-helices. With a cysteine at the C-terminus of each of the truncated proteins (H(1-47), H(1-54), H(1-59), H(1-61), H(1-67), H(1-69), H(1-71), H(1-78), H(1-80), H(1-91), and H(47-105)), the residues involved in formation of the coiled-coil interface were determined. Proteins H(1-54), H(1-61), H(1-69), and H(1-80) showed strong cross-link formation, which was weaker in H(1-47), H(1-59), H(1-71), and H(1-91). A shift in disulfide formation between cysteines at positions 71 and 80 reflected an interruption in the periodicity of hydrophobic residues in the region 71AEKILEETEKE81. To understand how the N-terminal domain of H is formed, we determined for the first time, to our knowledge, the solution NMR structure of H(1-47), which revealed an alpha-helix between residues 15-42 and a flexible N-terminal stretch. The alpha-helix includes a kink that would bring the two helices of the C-terminus into the coiled-coil arrangement. H(1-47) revealed a strip of alanines involved in dimerization, which were tested by exchange to single cysteines in subunit H mutants. PubMed: 19580766DOI: 10.1016/j.bpj.2009.04.026 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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