title: N-terminal amino acid sequencing of EDP208 conjugative pili.
abstract: EDP208 conjugative pili contain a single polypeptide subunit of 11,500 daltons with a blocked N-terminus. This N-terminal blocking moiety was identified as an N-acetyl group by 1H nuclear magnetic resonance analysis of an N-terminal tripeptide isolated from pronase digests of EDP208 pilin. Limited acid hydrolysis of the tripeptide allowed its sequence to be determined as acetyl-NH-Thr-Asp-Leu. Trypsin digestion of EDP208 pilin resulted in the quantitative release of a fragment containing 12 residues from the N-terminus of the protein. The sequence of this dodecapeptide was determined to be acetyl-NH-Thr-Asp-Leu-Leu-Ala-Gly-Gly-Lys-Asp-Val-Asp-Lys.
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D003227:Conjugation, Genetic; D004926:Escherichia coli / Q000648:ultrastructure*; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000032:analysis*; D008565:Membrane Proteins; D010455:Peptides; D014357:Trypsin
chemical_list: D001426:Bacterial Proteins; D008565:Membrane Proteins; D010455:Peptides; D036781:Fimbriae Proteins; D014357:Trypsin