Crystal structure of AtTTM3 in complex with tripolyphosphate and manganese ion (form A)Crystal structure of AtTTM3 in complex with tripolyphosphate and manganese ion (form A)

Structural highlights

5a66 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[TTM3_ARATH] 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), however it does not display significant activity towards long-chain polyphosphates. The existence of PPPi in living cells is still unclear, and PPPase activity might be the ancestral function of CYTH domain. It also has gamma-phosphatase activity on NTP substrates, but no adenylate cyclase or RNA triphosphatase activity.[1]

References

  1. Moeder W, Garcia-Petit C, Ung H, Fucile G, Samuel MA, Christendat D, Yoshioka K. Crystal structure and biochemical analyses reveal that the Arabidopsis triphosphate tunnel metalloenzyme AtTTM3 is a tripolyphosphatase involved in root development. Plant J. 2013 Nov;76(4):615-26. doi: 10.1111/tpj.12325. Epub 2013 Oct 17. PMID:24004165 doi:http://dx.doi.org/10.1111/tpj.12325

5a66, resolution 2.05Å

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