3FVJ
Crystal structure of phospholipase A2 1B crystallized in the presence of octyl sulfate
Summary for 3FVJ
| Entry DOI | 10.2210/pdb3fvj/pdb |
| Related | 3FVI |
| Descriptor | Phospholipase A2, major isoenzyme, CALCIUM ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | phospholipase a2, pla2-1b, octyl sulfate binding, hydrolase, lipid degradation, lipoprotein, metal-binding, palmitate, pyrrolidone carboxylic acid, secreted |
| Biological source | Sus scrofa (pigs,swine,wild boar) |
| Cellular location | Secreted: P00592 |
| Total number of polymer chains | 1 |
| Total formula weight | 14125.32 |
| Authors | Pan, Y.H. (deposition date: 2009-01-15, release date: 2010-03-16, Last modification date: 2023-09-06) |
| Primary citation | Pan, Y.H.,Bahnson, B.J. Structure of a premicellar complex of alkyl sulfates with the interfacial binding surfaces of four subunits of phospholipase A2. Biochim.Biophys.Acta, 1804:1443-1448, 2010 Cited by PubMed Abstract: The properties of three discrete premicellar complexes (E1#, E2#, E3#) of pig pancreatic group-IB secreted phospholipase A2 (sPLA2) with monodisperse alkyl sulfates have been characterized [Berg, O. G. et al., Biochemistry 43, 7999-8013, 2004]. Here we have solved the 2.7 A crystal structure of group-IB sPLA2 complexed with 12 molecules of octyl sulfate (C8S) in a form consistent with a tetrameric oligomeric that exists during the E1# phase of premicellar complexes. The alkyl tails of the C8S molecules are centered in the middle of the tetrameric cluster of sPLA2 subunits. Three of the four sPLA2 subunits also contain a C8S molecule in the active site pocket. The sulfate oxygen of a C8S ligand is complexed to the active site calcium in three of the four protein active sites. The interactions of the alkyl sulfate head group with Arg-6 and Lys-10, as well as the backbone amide of Met-20, are analogous to those observed in the previously solved sPLA2 crystal structures with bound phosphate and sulfate anions. The cluster of three anions found in the present structure is postulated to be the site for nucleating the binding of anionic amphiphiles to the interfacial surface of the protein, and therefore this binding interaction has implications for interfacial activation of the enzyme. PubMed: 20302975DOI: 10.1016/j.bbapap.2010.03.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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