2KHK
NMR solution structure of the b30-82 domain of subunit b of Escherichia coli F1FO ATP synthase
Summary for 2KHK
| Entry DOI | 10.2210/pdb2khk/pdb |
| NMR Information | BMRB: 16247 |
| Descriptor | ATP synthase subunit b (1 entity in total) |
| Functional Keywords | b30-82, f1fo atp synthase, nmr spectroscopy, atp synthesis, cell inner membrane, cell membrane, cf(0), hydrogen ion transport, ion transport, membrane, transmembrane, transport, transport protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 5785.63 |
| Authors | Priya, R.,Biukovic, G.,Gayen, S.,Vivekanandan, S.,Gruber, G. (deposition date: 2009-04-08, release date: 2009-12-15, Last modification date: 2024-05-15) |
| Primary citation | Priya, R.,Biukovic, G.,Gayen, S.,Vivekanandan, S.,Gruber, G. Solution structure, determined by nuclear magnetic resonance, of the b30-82 domain of subunit b of Escherichia coli F1Fo ATP synthase J.Bacteriol., 191:7538-7544, 2009 Cited by PubMed Abstract: Subunit b, the peripheral stalk of bacterial F(1)F(o) ATP synthases, is composed of a membrane-spanning and a soluble part. The soluble part is divided into tether, dimerization, and delta-binding domains. The first solution structure of b30-82, including the tether region and part of the dimerization domain, has been solved by nuclear magnetic resonance, revealing an alpha-helix between residues 39 and 72. In the solution structure, b30-82 has a length of 48.07 A. The surface charge distribution of b30-82 shows one side with a hydrophobic surface pattern, formed by alanine residues. Alanine residues 61, 68, 70, and 72 were replaced by single cysteines in the soluble part of subunit b, b22-156. The cysteines at positions 61, 68, and 72 showed disulfide formation. In contrast, no cross-link could be formed for the A70C mutant. The patterns of disulfide bonding, together with the circular dichroism spectroscopy data, are indicative of an adjacent arrangement of residues 61, 68, and 72 in both alpha-helices in b22-156. PubMed: 19820091DOI: 10.1128/JB.00540-09 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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