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==Structure of spermidine N-acetyltransferase SpeG from Vibrio cholerae==
==Structure of spermidine N-acetyltransferase SpeG from Vibrio cholerae==
<StructureSection load='5ug4' size='340' side='right' caption='[[5ug4]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='5ug4' size='340' side='right'caption='[[5ug4]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ug4]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UG4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UG4 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ug4]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae_01 Vibrio cholerae 01]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UG4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5UG4 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=MOH:METHANOL'>MOH</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">speG, VC_A0947 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=127906 Vibrio cholerae 01])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diamine_N-acetyltransferase Diamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.57 2.3.1.57] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diamine_N-acetyltransferase Diamine N-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.57 2.3.1.57] </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=5ug4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ug4 OCA], [http://pdbe.org/5ug4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ug4 RCSB], [http://www.ebi.ac.uk/pdbsum/5ug4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ug4 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ug4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ug4 OCA], [http://pdbe.org/5ug4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ug4 RCSB], [http://www.ebi.ac.uk/pdbsum/5ug4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ug4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ATDA_VIBCH 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.<ref>PMID:23184347</ref> <ref>PMID:25623305</ref>   
[[http://www.uniprot.org/uniprot/ATDA_VIBCH 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.<ref>PMID:23184347</ref> <ref>PMID:25623305</ref>   
==See Also==
*[[Spermidine/spermine N-acetyltransferase|Spermidine/spermine N-acetyltransferase]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Diamine N-acetyltransferase]]
[[Category: Diamine N-acetyltransferase]]
[[Category: Large Structures]]
[[Category: Vibrio cholerae 01]]
[[Category: Anderson, W F]]
[[Category: Anderson, W F]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]

Revision as of 15:35, 23 September 2020

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 01. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , ,
Gene:speG, VC_A0947 (Vibrio cholerae 01)
Activity:Diamine N-acetyltransferase, with EC number 2.3.1.57
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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