2CZT
lipocalin-type prostaglandin D synthase
Summary for 2CZT
| Entry DOI | 10.2210/pdb2czt/pdb |
| Related | 2CZU |
| Descriptor | Prostaglandin-H2 D-isomerase (2 entities in total) |
| Functional Keywords | lipocalin, c2221 native, riken structural genomics/proteomics initiative, rsgi, structural genomics, isomerase |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Rough endoplasmic reticulum (By similarity): O09114 |
| Total number of polymer chains | 1 |
| Total formula weight | 18617.86 |
| Authors | Kumasaka, T.,Irikura, D.,Ago, H.,Aritake, K.,Yamamoto, M.,Inoue, T.,Miyano, M.,Urade, Y.,Hayaishi, O.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-07-17, release date: 2006-10-03, Last modification date: 2024-10-16) |
| Primary citation | Kumasaka, T.,Aritake, K.,Ago, H.,Irikura, D.,Tsurumura, T.,Yamamoto, M.,Miyano, M.,Urade, Y.,Hayaishi, O. Structural basis of the catalytic mechanism operating in open-closed conformers of lipocalin type prostaglandin D synthase. J.Biol.Chem., 284:22344-22352, 2009 Cited by PubMed Abstract: Lipocalin type prostaglandin D synthase (L-PGDS) is a multifunctional protein acting as a somnogen (PGD2)-producing enzyme, an extracellular transporter of various lipophilic ligands, and an amyloid-beta chaperone in human cerebrospinal fluid. In this study, we determined the crystal structures of two different conformers of mouse L-PGDS, one with an open cavity of the beta-barrel and the other with a closed cavity due to the movement of the flexible E-F loop. The upper compartment of the central large cavity contains the catalytically essential Cys65 residue and its network of hydrogen bonds with the polar residues Ser45, Thr67, and Ser81, whereas the lower compartment is composed of hydrophobic amino acid residues that are highly conserved among other lipocalins. SH titration analysis combined with site-directed mutagenesis revealed that the Cys65 residue is activated by its interaction with Ser45 and Thr67 and that the S45A/T67A/S81A mutant showed less than 10% of the L-PGDS activity. The conformational change between the open and closed states of the cavity indicates that the mobile calyx contributes to the multiligand binding ability of L-PGDS. PubMed: 19546224DOI: 10.1074/jbc.M109.018341 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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