2AIZ

Solution structure of peptidoglycan associated lipoprotein from Haemophilus influenza bound to UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine

Summary for 2AIZ

• Entry DOI: 10.2210/pdb2aiz/pdb
• NMR Information: BMRB: 6465,6856,6858
• Descriptor: Outer membrane protein P6 (Fragment), L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine, N-acetyl-beta-muramic acid, ... (4 entities in total)
• Functional Keywords: alpha-beta sandwich, structure 2 function project, s2f, structural genomics, membrane protein
• Biological source: Haemophilus influenzae; More
• Cellular location: Cell outer membrane; Lipid-anchor: M4PH67
• Total number of polymer chains: 2
• Total formula weight: 15481.55

Authors

Parsons, L.M.,Lin, F.,Orban, J.,Structure 2 Function Project (S2F) (deposition date: 2005-08-01, release date: 2006-03-14, Last modification date: 2024-10-30)

Primary citation

Parsons, L.M.,Lin, F.,Orban, J.
Peptidoglycan recognition by pal, an outer membrane lipoprotein.
Biochemistry, 45:2122-2128, 2006

PubMed Abstract: Peptidoglycan-associated lipoprotein (Pal) is a potential vaccine candidate from Haemophilus influenzae that is highly conserved in Gram-negative bacteria and anchored to the outer membrane through an N-terminal lipid attachment. Pal stabilizes the outer membrane by providing a noncovalent link to the peptidoglycan (PG) layer through a periplasmic domain. Using NMR spectroscopy, we determined the three-dimensional structure of a complex between the periplasmic domain of Pal and a biosynthetic peptidoglycan precursor (PG-P), UDP-N-acetylmuramyl-L-Ala-alpha-d-Glu-m-Dap-D-Ala-d-Ala (m-Dap is meso-diaminopimelate). Pal has a binding pocket lined with conserved surface residues that interacts exclusively with the peptide portion of the ligand. The m-Dap residue, which is mainly found in the cell walls of Gram-negative bacteria, is sequestered in this pocket and plays an important role by forming hydrogen bond and hydrophobic contacts to Pal. The structure provides insight into the mode of cell wall recognition for a broad class of Gram-negative membrane proteins, including OmpA and MotB, which have peptidoglycan-binding domains homologous to that of Pal.

PubMed: 16475801
DOI: 10.1021/bi052227i

Experimental method

SOLUTION NMR