4JEP
Crystal structure of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase 1 (NTPDase1)
Summary for 4JEP
Entry DOI | 10.2210/pdb4jep/pdb |
Related | 4A57 4A59 4A5A 4A5B |
Descriptor | Nucleoside-triphosphatase 2 (1 entity in total) |
Functional Keywords | hydrolase, phosphatase, ntpdase |
Biological source | Toxoplasma gondii |
Cellular location | Secreted: Q27895 |
Total number of polymer chains | 2 |
Total formula weight | 136152.42 |
Authors | Krug, U.,Totzauer, R.,Strater, N. (deposition date: 2013-02-27, release date: 2013-04-10, Last modification date: 2017-11-15) |
Primary citation | Krug, U.,Totzauer, R.,Strater, N. The crystal structure of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase 1 represents a conformational intermediate in the reductive activation mechanism of the tetrameric enzyme. Proteins, 81:1271-1276, 2013 Cited by PubMed Abstract: Toxoplasma gondii nucleoside triphosphate diphosphohydrolase (NTPDase) 1 was crystallized in an intermediate tetrameric conformation. The crystal structure is similar to that of T. gondii NTPDase3 and represents an inactive conformation as the activating disulfide bridge is not reduced and the active site cleft between the two domains of each monomer is open. However, the arrangement of the monomers within the tetramer differs from that of the inactive form of NTPDase3 and may represent an intermediate conformation on the path of the closure motion of the tetramer induced upon activation. PubMed: 23526564DOI: 10.1002/prot.24288 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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