Crystal Structure of a T.thermophilus HB8 Ap6A Hydrolase Ndx1-Ap6A ComplexCrystal Structure of a T.thermophilus HB8 Ap6A Hydrolase Ndx1-Ap6A Complex
Structural highlights
1vc8 is a 2 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NDX1_THETH Specifically hydrolyzes (di)adenosine polyphosphates but not ATP or diadenosine triphosphate, generating ATP as the product. Diadenosine hexaphosphate (Ap6A) is the preferred substrate and its hydrolyzation yields 2 ATP. It is the only enzyme that symmetrically hydrolyzes Ap6A. It also hydrolyzes diadenosine pentaphosphate (Ap5A), diadenosine tetraphosphate (Ap4A), adenosine tetraphosphate (p4A) to produce ATP and ADP, ATP and AMP, ATP and inorganic orthophosphate, respectively.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
↑Iwai T, Kuramitsu S, Masui R. The Nudix hydrolase Ndx1 from Thermus thermophilus HB8 is a diadenosine hexaphosphate hydrolase with a novel activity. J Biol Chem. 2004 May 21;279(21):21732-9. Epub 2004 Mar 15. PMID:15024014 doi:http://dx.doi.org/10.1074/jbc.M312018200