The crystal structure and oligomeric form of Escherichia colil,d-carboxypeptidase A.

摘要: Abstract Bacterial peptidoglycan is constructed by cross-linking sugar chains carrying pentapeptide building blocks with two d -alanine residues at the C-terminus. Incorporation into polymer and subsequent breakdown of releases a tetrapeptide single residue. Removal this residue necessary for tripeptide to receive new D-Ala-D-Ala dipeptide in synthetic pathway, but proteases are generally unable work substrates having unusual chirality close scissile bond. Processing carried out dedicated ld -carboxypeptidase, which interest as novel drug target. We describe high resolution crystal structure enzyme from E. coli, demonstrate dimeric highly conserved.