Isopeptide linkage between N-alpha-monomethylalanine and lysine in ribosomal protein S11 from Escherichia coli.
Protein S11 from the Escherichia coli ribosome has a unique NH2-terminal structure not previously observed among ribosomal proteins. Owing to the formation of an isopeptide bond between a secondary amino acid (N-alpha-monomethylalanine) and the epsilon-amino group of the NH2-terminal lysine residue, a "branching point" is formed. Therefore, two amino acids are seen when the NH2 terminus of the protein is determined.
D000409:Alanine / Q000031:analogs & derivatives* / Q000032:analysis; D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D055598:Chemical Phenomena; D002621:Chemistry; D004926:Escherichia coli / Q000032:analysis*; D006868:Hydrolysis; D007931:Leucyl Aminopeptidase; D008239:Lysine / Q000032:analysis*; D009842:Oligopeptides / Q000138:chemical synthesis; D012269:Ribosomal Proteins; D014357:Trypsin
D001426:Bacterial Proteins; D009842:Oligopeptides; D012269:Ribosomal Proteins; D007931:Leucyl Aminopeptidase; D014357:Trypsin; D008239:Lysine; D000409:Alanine