Back to Search
Start Over
Solution Structure, Determined by Nuclear Magnetic Resonance, of the b30-82 Domain of Subunit b of Escherichia coli F 1 F o ATP Synthase
- Source :
- Journal of Bacteriology. 191:7538-7544
- Publication Year :
- 2009
- Publisher :
- American Society for Microbiology, 2009.
-
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 δ-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 α-helix between residues 39 and 72. In the solution structure, b30-82 has a length of 48.07 Å. 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 α-helices in b22-156.
- Subjects :
- Models, Molecular
Alanine
Circular dichroism
ATP synthase
biology
Circular Dichroism
Protein subunit
Static Electricity
Mutant
medicine.disease_cause
Microbiology
Protein Structure, Secondary
Protein Structure, Tertiary
Protein Subunits
Nuclear magnetic resonance
Protein structure
Structural Biology
Bacterial Proton-Translocating ATPases
Static electricity
Escherichia coli
biology.protein
medicine
Nuclear Magnetic Resonance, Biomolecular
Molecular Biology
Subjects
Details
- ISSN :
- 10985530 and 00219193
- Volume :
- 191
- Database :
- OpenAIRE
- Journal :
- Journal of Bacteriology
- Accession number :
- edsair.doi.dedup.....05fbf11fd288a88cea711e3df73e6132