==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==

<StructureSection load='2aiz' size='340' side='right' caption='[[2aiz]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[2aiz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AIZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AIZ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMU:BETA-N-ACETYLMURAMIC+ACID'>AMU</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2aiz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aiz OCA], [http://pdbe.org/2aiz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2aiz RCSB], [http://www.ebi.ac.uk/pdbsum/2aiz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2aiz ProSAT]</span></td></tr>

== Function ==

[[http://www.uniprot.org/uniprot/PAL_HAEIN PAL_HAEIN]] Thought to play a role in bacterial envelope integrity. Links the outer membrane to the peptidoglycan layer.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

Peptidoglycan recognition by Pal, an outer membrane lipoprotein.,Parsons LM, Lin F, Orban J Biochemistry. 2006 Feb 21;45(7):2122-8. PMID:16475801<ref>PMID:16475801</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2aiz" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacterium influenzae lehmann and neumann 1896]]

[[Category: Lin, F]]

[[Category: Alpha-beta sandwich]]

[[Category: Structure 2 function project]]