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2JOB

Solution structure of an antilipopolysaccharide factor from shrimp and its possible Lipid A binding site

Summary for 2JOB
Entry DOI10.2210/pdb2job/pdb
NMR InformationBMRB: 15622
Descriptorantilipopolysaccharide factor (1 entity in total)
Functional Keywordsalf, lipid a binding protein, endotoxin, lipid binding protein
Biological sourcePenaeus monodon (black tiger shrimp)
Total number of polymer chains1
Total formula weight11532.19
Authors
Yang, Y.,Boze, H.,Chemardin, P.,Padilla, A.,Moulin, G.,Tassanakajon, A.,Pugniere, M.,Roquet, F.,Gueguen, Y.,Bachere, E.,Aumelas, A. (deposition date: 2007-03-02, release date: 2008-03-11, Last modification date: 2024-11-06)
Primary citationYang, Y.,Boze, H.,Chemardin, P.,Padilla, A.,Moulin, G.,Tassanakajon, A.,Pugniere, M.,Roquet, F.,Destoumieux-Garzon, D.,Gueguen, Y.,Bachere, E.,Aumelas, A.
NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: Model of the possible lipid A-binding site
Biopolymers, 91:207-220, 2009
Cited by
PubMed Abstract: The anti-lipopolysaccharide factor ALF-Pm3 is a 98-residue protein identified in hemocytes from the black tiger shrimp Penaeus monodon. It was expressed in Pichia pastoris from the constitutive glyceraldehyde-3-phosphate dehydrogenase promoter as a folded and (15)N uniformly labeled rALF-Pm3 protein. Its 3D structure was established by NMR and consists of three alpha-helices packed against a four-stranded beta-sheet. The C(34)-C(55) disulfide bond was shown to be essential for the structure stability. By using surface plasmon resonance, we demonstrated that rALF-Pm3 binds to LPS, lipid A and to OM-174, a soluble analogue of lipid A. Biophysical studies of rALF-Pm3/LPS and rALF-Pm3/OM-174 complexes indicated rather high molecular sized aggregates, which prevented us to experimentally determine by NMR the binding mode of these lipids to rALF-Pm3. However, on the basis of striking structural similarities to the FhuA/LPS complex, we designed an original model of the possible lipid A-binding site of ALF-Pm3. Such a binding site, located on the ALF-Pm3 beta-sheet and involving seven charged residues, is well conserved in ALF-L from Limulus polyphemus and in ALF-T from Tachypleus tridentatus. In addition, our model is in agreement with experiments showing that beta-hairpin synthetic peptides corresponding to ALF-L beta-sheet bind to LPS. Delineating lipid A-binding site of ALFs will help go further in the de novo design of new antibacterial or LPS-neutralizing drugs.
PubMed: 19107926
DOI: 10.1002/bip.21119
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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