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NMR investigations of the structural properties of the nodulation protein, NodF, from Rhizobium leguminosarum and its homology with Escherichia coli acyl carrier protein
- Source :
- FEBS Letters. (1):66-72
- Publisher :
- Published by Elsevier B.V.
-
Abstract
- Heteronuclear NMR methods have been used to elucidate the secondary structure and the general tertiary fold of the protein NodF from Rhizobium leguminosarum. A similarity to acyl carrier proteins of the fatty acid synthase system had been suggested by the presence of a phosphopantetheine prosthetic group and a short stretch of sequence homology near the prosthetic group attachment site. NMR results suggest that the structural homology extends well beyond this region. Both proteins have three well-formed helices which fold in a parallel-antiparallel fashion and a prosthetic group attachment site near the beginning of the second helix.
- Subjects :
- Protein Folding
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Biophysics
Nodulation factor
Biology
medicine.disease_cause
Biochemistry
Protein Structure, Secondary
Homology (biology)
Rhizobium leguminosarum
Cofactor
chemistry.chemical_compound
Bacterial Proteins
Structural Biology
Secondary structure
Escherichia coli
Genetics
medicine
Amino Acid Sequence
Acyl carrier protein
Molecular Biology
Protein secondary structure
Sequence Homology, Amino Acid
Cell Biology
NMR
Fatty acid synthase
chemistry
Fatty acid synthesis
Pantetheine
Helix
biology.protein
Phosphopantetheine
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....207482dfd023ab2c1e0defc4c25c581a
- Full Text :
- https://doi.org/10.1016/0014-5793(96)00512-1