PMID:9208918
| Citation |
Beglova, N, Fischer, D, Hengge-Aronis, R and Gehring, K (1997) 1H, 15N and 13C NMR assignments, secondary structure and overall topology of the Escherichia coli GlgS protein. Eur. J. Biochem. 246:301-10 |
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| Abstract |
GlgS is a 7892-Da protein which is involved in glycogen biosynthesis in bacteria. We report the 1H, 15N and 13C NMR assignments of the backbone and side-chain resonances at 25 degrees C and pH 6.7 from two-dimensional homonuclear and three-dimensional heteronuclear NMR experiments. The secondary structure of the protein was determined using sequential and medium-range NOE correlations, vicinal 3J(NH-H alpha) coupling values and amide proton exchange rates. The secondary structure obtained is consistent with the secondary chemical shifts of 1H alpha, 13C alpha and 13C = O. It was found that the secondary structure of GlgS comprises two amphipathic helices (Asn10-Met21 and Glu39-Arg60), one short highly hydrophobic helix (Ile30-Val33), a short extended beta-strand-like fragment (Arg26-Asp29) and two type I beta-turns (His22-Gly25 and Thr34-Met37). An overall topology of GlgS is suggested based on long-range NOEs. The elements of secondary structure form a sandwich in which the beta-strand and the short hydrophobic helix are positioned between the two amphipathic helices. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/isolation & purification; Carbon Isotopes; Chromatography, Gel; Escherichia coli/chemistry; Escherichia coli Proteins; Magnetic Resonance Spectroscopy; Mass Spectrometry; Molecular Sequence Data; Nitrogen Isotopes; Protein Structure, Secondary; Protons; Recombinant Proteins/chemistry; Recombinant Proteins/isolation & purification |
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