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Demonstration of segmental mobility in the functionally essential car☐yl terminal part of ribonucleotide reductase protein R2 from Escherichia coli
Author(s) -
PerOlof Lycksell,
Margareta Sahlin
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00706-f
Subject(s) - ribonucleotide reductase , escherichia coli , mutant , chemistry , biochemistry , c terminus , amino acid , n terminus , stereochemistry , peptide sequence , protein subunit , gene
The C‐terminus of protein R2 is important for the formation of the enzymatically active complex between proteins R1 and R2 of ribonucleotide reductase from Escherichia coli . Some residues in this part of R2 may also be involved in intramolecular electron transfer. We now demonstrate that 26 amino acid residues at C‐terminus of protein R2 are mobile in the free protein, and can be studied by 1 H NMR. Spectral assignment of narrow resonances was made by comparison of TOCSY and NOESY spectra from wild‐type R2 with corresponding spectra of a mutant protein R2, lacking 30 residues at the car☐yl terminus.