7JTV

Structure of IMPa from Pseudomonas aeruginosa in complex with an O-glycopeptide

Summary for 7JTV

• Entry DOI: 10.2210/pdb7jtv/pdb
• Descriptor: Immunomodulating metalloprotease, GLU-ALA-PRO-SER-ALA, beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-galactopyranose, ... (6 entities in total)
• Functional Keywords: o-glycopeptidase, glycopeptidase, glycopeptide, pseudomonas aeruginosa, impa, peptidase_m60, m88 peptidase, gluzincin, protein binding
• Biological source: Pseudomonas aeruginosa; More
• Total number of polymer chains: 4
• Total formula weight: 196899.47

Authors

Noach, I.,Boraston, A.B. (deposition date: 2020-08-18, release date: 2020-12-16, Last modification date: 2024-10-30)

Primary citation

Noach, I.,Boraston, A.B.
Structural evidence for a proline-specific glycopeptide recognition domain in an O-glycopeptidase.
Glycobiology, 31:385-390, 2021

PubMed Abstract: The glycosylation of proteins is typically considered as a stabilizing modification, including resistance to proteolysis. A class of peptidases, referred to as glycopeptidases or O-glycopeptidases, circumvent the protective effect of glycans against proteolysis by accommodating the glycans in their active sites as specific features of substrate recognition. IMPa from Pseudomonas aeruginosa is such an O-glycopeptidase that cleaves the peptide bond immediately preceding a site of O-glycosylation, and through this glycoprotein-degrading function contributes to the host-pathogen interaction. IMPa, however, is a relatively large multidomain protein and how its additional domains may contribute to its function remains unknown. Here, through the determination of a crystal structure of IMPa in complex with an O-glycopeptide, we reveal that the N-terminal domain of IMPa, which is classified in Pfam as IMPa_N_2, is a proline recognition domain that also shows the properties of recognizing an O-linked glycan on the serine/threonine residue following the proline. The proline is bound in the center of a bowl formed by four functionally conserved aromatic amino acid side chains while the glycan wraps around one of the tyrosine residues in the bowl to make classic aromatic ring-carbohydrate CH-π interactions. This structural evidence provides unprecedented insight into how the ancillary domains in glycoprotein-specific peptidases can noncatalytically recognize specific glycosylated motifs that are common in mucin and mucin-like molecules.

PubMed: 33030205
DOI: 10.1093/glycob/cwaa095

Experimental method

X-RAY DIFFRACTION (2.45 Å)