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Topology of the secondary structure elements of ribosomal protein L7/L12 from E. coli in solution
Author(s) -
Bocharov E.V.,
Gudkov A.T.,
Arseniev A.S.
Publication year - 1996
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)01531-0
Subject(s) - antiparallel (mathematics) , dimer , ribosomal protein , protein secondary structure , crystallography , chemistry , ribosomal rna , stereochemistry , helix (gastropod) , protein structure , topology (electrical circuits) , helix bundle , resolution (logic) , peptide bond , peptide , biology , rna , physics , biochemistry , ribosome , gene , ecology , mathematics , organic chemistry , quantum mechanics , combinatorics , artificial intelligence , snail , magnetic field , computer science
Topology of the secondary structure elements of ribosomal protein L7/L12 has been studied. The sequential assignment was obtained for main and side chain resonances. This allows the overall secondary structure to be described. The results of high resolution NMR studies show that dimer of the ribosomal protein L7/L12 from Escherichia coli has a parallel (head‐to‐head) orientation of subunits, and N‐terminal domain (NTD, residues Ser1‐Ser33) has no contracts with the C‐terminal domain (CTD, residues Lys51‐Lys120). The NMR data for CTD are in line with crystallographic structure. The flexible interdomain (hinge) region (residues Ala34‐Glu50) has an unordered structure, the Pro44 forming both cis and trans peptide bonds. Due to the conformational exchange the intensities of the peaks from the NTD are low. The conformation of the NTD, which is responsible for the formation of the L7/L12 dimer, is α‐helical hairpin. The NTD dimer forms an antiparallel four‐α‐helix bundle.