Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4BPA

Crystal structure of AmpDh2 from Pseudomonas aeruginosa in complex with NAG-NAM-NAG-NAM tetrasaccharide

Summary for 4BPA
Entry DOI10.2210/pdb4bpa/pdb
Related4BOL
DescriptorAMPDH2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-N-acetyl-beta-muramic acid-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-methyl 2-acetamido-3-O-[(1R)-1-carboxyethyl]-2-deoxy-beta-D-glucopyranoside, ZINC ION, ... (4 entities in total)
Functional Keywordshydrolase
Biological sourcePSEUDOMONAS AERUGINOSA PAO1
Total number of polymer chains2
Total formula weight58951.29
Authors
Primary citationMartinez-Caballero, S.,Lee, M.,Artola-Recolons, C.,Carrasco-Lopez, C.,Hesek, D.,Spink, E.E.,Lastochkin, E.,Zhang, W.,Hellman, L.M.,Boggess, B.,Mobashery, S.,Hermoso, J.A.
Reaction Products and the X-Ray Structure of Ampdh2, a Virulence Determinant of Pseudomonas Aeruginosa.
J.Am.Chem.Soc., 135:10318-, 2013
Cited by
PubMed Abstract: The zinc protease AmpDh2 is a virulence determinant of Pseudomonas aeruginosa, a problematic human pathogen. The mechanism of how the protease manifests virulence is not known, but it is known that it turns over the bacterial cell wall. The reaction of AmpDh2 with the cell wall was investigated, and nine distinct turnover products were characterized by LC/MS/MS. The enzyme turns over both the cross-linked and noncross-linked cell wall. Three high-resolution X-ray structures, the apo enzyme and two complexes with turnover products, were solved. The X-ray structures show how the dimeric protein interacts with the inner leaflet of the bacterial outer membrane and that the two monomers provide a more expansive surface for recognition of the cell wall. This binding surface can accommodate the 3D solution structure of the cross-linked cell wall.
PubMed: 23819763
DOI: 10.1021/JA405464B
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon