 |
PDBsum entry 2aiz
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Membrane protein
|
PDB id
|
|
|
|
2aiz
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Peptidoglycan recognition by pal, An outer membrane lipoprotein.
|
|
|
Authors
|
|
L.M.Parsons,
F.Lin,
J.Orban.
|
|
|
Ref.
|
|
Biochemistry, 2006,
45,
2122-2128.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
