2JOB
Solution structure of an antilipopolysaccharide factor from shrimp and its possible Lipid A binding site
Summary for 2JOB
| Entry DOI | 10.2210/pdb2job/pdb |
| NMR Information | BMRB: 15622 |
| Descriptor | antilipopolysaccharide factor (1 entity in total) |
| Functional Keywords | alf, lipid a binding protein, endotoxin, lipid binding protein |
| Biological source | Penaeus monodon (black tiger shrimp) |
| Total number of polymer chains | 1 |
| Total formula weight | 11532.19 |
| 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 citation | Yang, 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: 19107926DOI: 10.1002/bip.21119 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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