1PD2

CRYSTAL STRUCTURE OF HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE COMPLEX WITH GLUTATHIONE

Summary for 1PD2

• Entry DOI: 10.2210/pdb1pd2/pdb
• Descriptor: HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE, GLUTATHIONE (3 entities in total)
• Functional Keywords: hematopoietic prostaglandin d synthase, pgds, gst, sigma-class gst, ligase
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Cytoplasm: O35543
• Total number of polymer chains: 2
• Total formula weight: 47262.53

Authors

Miyano, M.,Ago, H. (deposition date: 1998-12-14, release date: 1999-10-13, Last modification date: 2023-12-27)

Primary citation

Kanaoka, Y.,Ago, H.,Inagaki, E.,Nanayama, T.,Miyano, M.,Kikuno, R.,Fujii, Y.,Eguchi, N.,Toh, H.,Urade, Y.,Hayaishi, O.
Cloning and crystal structure of hematopoietic prostaglandin D synthase.
Cell(Cambridge,Mass.), 90:1085-1095, 1997

PubMed Abstract: Hematopoietic prostaglandin (PG) D synthase is the key enzyme for production of the D and J series of prostanoids in the immune system and mast cells. We isolated a cDNA for the rat enzyme, crystallized the recombinant enzyme, and determined the three-dimensional structure of the enzyme complexed with glutathione at 2.3 A resolution. The enzyme is the first member of the sigma class glutathione S-transferase (GST) from vertebrates and possesses a prominent cleft as the active site, which is never seen among other members of the GST family. The unique 3-D architecture of the cleft leads to the putative substrate binding mode and its catalytic mechanism, responsible for the specific isomerization from PGH2 to PGD2.

PubMed: 9323136
DOI: 10.1016/S0092-8674(00)80374-8

Experimental method

X-RAY DIFFRACTION (2.3 Å)