5ug4

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Structure of spermidine N-acetyltransferase SpeG from Vibrio choleraeStructure of spermidine N-acetyltransferase SpeG from Vibrio cholerae

Structural highlights

5ug4 is a 3 chain structure with sequence from Vibrio cholerae O1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ATDA_VIBCH Involved in the protection against polyamine toxicity by regulating their concentration. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amino groups of spermidine to yield N(1)- and N(8)-acetylspermidine. It can use polyamines such as spermine and N(1)-acetylspermine, but not putrescine or cadaverine.[1] [2]

See Also

References

  1. Kuhn ML, Majorek KA, Minor W, Anderson WF. Broad-substrate screen as a tool to identify substrates for bacterial Gcn5-related N-acetyltransferases with unknown substrate specificity. Protein Sci. 2013 Feb;22(2):222-30. doi: 10.1002/pro.2199. Epub 2012 Dec 17. PMID:23184347 doi:http://dx.doi.org/10.1002/pro.2199
  2. Filippova EV, Kuhn ML, Osipiuk J, Kiryukhina O, Joachimiak A, Ballicora MA, Anderson WF. A Novel Polyamine Allosteric Site of SpeG from Vibrio cholerae Is Revealed by Its Dodecameric Structure. J Mol Biol. 2015 Mar 27;427(6 Pt B):1316-34. doi: 10.1016/j.jmb.2015.01.009. Epub, 2015 Jan 23. PMID:25623305 doi:http://dx.doi.org/10.1016/j.jmb.2015.01.009

5ug4, resolution 2.15Å

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OCA