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| | <StructureSection load='7kx3' size='340' side='right'caption='[[7kx3]], [[Resolution|resolution]] 2.67Å' scene=''> | | <StructureSection load='7kx3' size='340' side='right'caption='[[7kx3]], [[Resolution|resolution]] 2.67Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7kx3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KX3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7kx3]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7KX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7KX3 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">speG, VC_A0947 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.67Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Diamine_N-acetyltransferase Diamine N-acetyltransferase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=7kx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kx3 OCA], [https://pdbe.org/7kx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kx3 RCSB], [https://www.ebi.ac.uk/pdbsum/7kx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kx3 ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7kx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7kx3 OCA], [https://pdbe.org/7kx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7kx3 RCSB], [https://www.ebi.ac.uk/pdbsum/7kx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7kx3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://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>
| + | [https://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 7kx3" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 7kx3" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Spermidine/spermine N-acetyltransferase|Spermidine/spermine N-acetyltransferase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Diamine N-acetyltransferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Vibch]] | + | [[Category: Vibrio cholerae O1 biovar El Tor str. N16961]] |
| - | [[Category: Boeck, P]] | + | [[Category: Boeck P]] |
| - | [[Category: Forwood, J K]] | + | [[Category: Forwood JK]] |
| - | [[Category: Gawat, D]] | + | [[Category: Gawat D]] |
| - | [[Category: Kuhn, M L]] | + | [[Category: Kuhn ML]] |
| - | [[Category: Le, V T.B]] | + | [[Category: Le VTB]] |
| - | [[Category: Lim, E Q]] | + | [[Category: Lim EQ]] |
| - | [[Category: Renolo, R]] | + | [[Category: Renolo R]] |
| - | [[Category: Solis, A]] | + | [[Category: Solis A]] |
| - | [[Category: Tsimbalyuk, S]] | + | [[Category: Tsimbalyuk S]] |
| - | [[Category: Speg enzyme allosteric]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
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]
Publication Abstract from PubMed
Polyamines regulate many important biological processes including gene expression, intracellular signaling, and biofilm formation. Their intracellular concentrations are tightly regulated by polyamine transport systems and biosynthetic and catabolic pathways. Spermidine/spermine N-acetyltransferases (SSATs) are catabolic enzymes that acetylate polyamines and are critical for maintaining intracellular polyamine homeostasis. These enzymes belong to the Gcn5-related N-acetyltransferase (GNAT) superfamily and adopt a highly conserved fold found across all kingdoms of life. SpeG is an SSAT protein found in a variety of bacteria, including the human pathogen Vibrio cholerae. This protein adopts a dodecameric structure and contains an allosteric site, making it unique compared to other SSATs. Currently, we have a limited understanding of the critical structural components of this protein that are required for its allosteric behavior. Therefore, we explored the importance of two key regions of the SpeG protein on its kinetic activity. To achieve this, we created various constructs of the V. cholerae SpeG protein, including point mutations, a deletion, and chimeras with residues from the structurally distinct and non-allosteric human SSAT protein. We measured enzyme kinetic activity toward spermine for ten constructs and crystallized six of them. Ultimately, we identified specific portions of the allosteric loop and the beta6-beta7 structural elements that were critical for enzyme kinetic activity. These results provide a framework for further study of the structure/function relationship of SpeG enzymes from other organisms and clues toward the structural evolution of members of the GNAT family across domains of life.
The Vibrio cholerae SpeG Spermidine/Spermine N-Acetyltransferase Allosteric Loop and beta6-beta7 Structural Elements Are Critical for Kinetic Activity.,Le VTB, Tsimbalyuk S, Lim EQ, Solis A, Gawat D, Boeck P, Lim EQ, Renolo R, Forwood JK, Kuhn ML Front Mol Biosci. 2021 Apr 13;8:645768. doi: 10.3389/fmolb.2021.645768., eCollection 2021. PMID:33928120[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
- ↑ 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
- ↑ Le VTB, Tsimbalyuk S, Lim EQ, Solis A, Gawat D, Boeck P, Lim EQ, Renolo R, Forwood JK, Kuhn ML. The Vibrio cholerae SpeG Spermidine/Spermine N-Acetyltransferase Allosteric Loop and beta6-beta7 Structural Elements Are Critical for Kinetic Activity. Front Mol Biosci. 2021 Apr 13;8:645768. doi: 10.3389/fmolb.2021.645768., eCollection 2021. PMID:33928120 doi:http://dx.doi.org/10.3389/fmolb.2021.645768
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