3PCV
Crystal structure analysis of human leukotriene C4 synthase at 1.9 angstrom resolution
Summary for 3PCV
| Entry DOI | 10.2210/pdb3pcv/pdb |
| Related | 2PNO |
| Descriptor | Leukotriene C4 synthase, GLUTATHIONE, DODECYL-BETA-D-MALTOSIDE, ... (7 entities in total) |
| Functional Keywords | membrane protein, helix bundle, homo trimer, mgst, mapeg, lyase |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus outer membrane; Multi-pass membrane protein: Q16873 |
| Total number of polymer chains | 1 |
| Total formula weight | 23776.03 |
| Authors | Saino, H.,Ago, H.,Miyano, M. (deposition date: 2010-10-22, release date: 2011-03-16, Last modification date: 2023-11-01) |
| Primary citation | Saino, H.,Ukita, Y.,Ago, H.,Irikura, D.,Nisawa, A.,Ueno, G.,Yamamoto, M.,Kanaoka, Y.,Lam, B.K.,Austen, K.F.,Miyano, M. The catalytic architecture of leukotriene C4 synthase with two arginine residues J.Biol.Chem., 286:16392-16401, 2011 Cited by PubMed Abstract: Leukotriene (LT) C(4) and its metabolites, LTD(4) and LTE(4), are involved in the pathobiology of bronchial asthma. LTC(4) synthase is the nuclear membrane-embedded enzyme responsible for LTC(4) biosynthesis, catalyzing the conjugation of two substrates that have considerably different water solubility; that amphipathic LTA(4) as a derivative of arachidonic acid and a water-soluble glutathione (GSH). A previous crystal structure revealed important details of GSH binding and implied a GSH activating function for Arg-104. In addition, Arg-31 was also proposed to participate in the catalysis based on the putative LTA(4) binding model. In this study enzymatic assay with mutant enzymes demonstrates that Arg-104 is required for the binding and activation of GSH and that Arg-31 is needed for catalysis probably by activating the epoxide group of LTA(4). PubMed: 21454538DOI: 10.1074/jbc.M110.150177 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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