The crystal structure of the inorganic triphosphatase NE1496The crystal structure of the inorganic triphosphatase NE1496

Structural highlights

3typ is a 2 chain structure with sequence from Nitrosomonas europaea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

3PASE_NITEU Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi). The enzyme has a strong preference for linear PPPi compared with cyclic PPPi (cyclic trimetaphosphate) and to the linear P4. The longer chains polyphosphate are not hydrolyzed. It has only a slight thiamine triphosphatase (ThTPase) activity. Nucleoside triphosphatase activity is negligible in the presence of magnesium, but a small activity is observed in the presence of manganese, in particular with GTP.[1]

References

  1. Delvaux D, Murty MR, Gabelica V, Lakaye B, Lunin VV, Skarina T, Onopriyenko O, Kohn G, Wins P, De Pauw E, Bettendorff L. A specific inorganic triphosphatase from Nitrosomonas europaea: structure and catalytic mechanism. J Biol Chem. 2011 Sep 30;286(39):34023-35. Epub 2011 Aug 12. PMID:21840996 doi:10.1074/jbc.M111.233585

3typ, resolution 1.90Å

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