3v85: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3v85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v85 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v85 RCSB], [http://www.ebi.ac.uk/pdbsum/3v85 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3v85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v85 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3v85 RCSB], [http://www.ebi.ac.uk/pdbsum/3v85 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/Q9SIY3_ARATH Q9SIY3_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.<ref>PMID:24004165</ref> 
== References ==
<references/>
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Revision as of 23:58, 25 December 2014

1.9 Angstrom resolution crystal structure of the protein Q9SIY3 from Arabidopsis thaliana1.9 Angstrom resolution crystal structure of the protein Q9SIY3 from Arabidopsis thaliana

Structural highlights

3v85 is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:At2g11890 (Arabidopsis thaliana)
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[Q9SIY3_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

3v85, resolution 1.90Å

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