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| | <StructureSection load='6cy6' size='340' side='right'caption='[[6cy6]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='6cy6' size='340' side='right'caption='[[6cy6]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6cy6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CY6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CY6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6cy6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CY6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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]] 1.75Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">speG, b1584, JW1576 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=6cy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cy6 OCA], [https://pdbe.org/6cy6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cy6 RCSB], [https://www.ebi.ac.uk/pdbsum/6cy6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cy6 ProSAT]</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=6cy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cy6 OCA], [http://pdbe.org/6cy6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cy6 RCSB], [http://www.ebi.ac.uk/pdbsum/6cy6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cy6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ATDA_ECOLI ATDA_ECOLI]] Regulates polyamine concentration by their degradation. Acts on spermidine, forming N(1)- and N(8)-acetylspermidine. | + | [https://www.uniprot.org/uniprot/ATDA_ECOLI ATDA_ECOLI] Regulates polyamine concentration by their degradation. Acts on spermidine, forming N(1)- and N(8)-acetylspermidine. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Diamine N-acetyltransferase]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Ecoli]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Anderson, W F]] | + | [[Category: Anderson WF]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Filippova EV]] |
| - | [[Category: Filippova, E V]] | + | [[Category: Joachimiak A]] |
| - | [[Category: Joachimiak, A]] | + | [[Category: Kiryukhina O]] |
| - | [[Category: Kiryukhina, O]] | + | [[Category: Minasov G]] |
| - | [[Category: Minasov, G]] | + | [[Category: Satchell KJF]] |
| - | [[Category: Satchell, K J.F]] | + | |
| - | [[Category: Csgid]]
| + | |
| - | [[Category: Gnat]]
| + | |
| - | [[Category: N-acetyltransferase]]
| + | |
| - | [[Category: Speg]]
| + | |
| - | [[Category: Spermidine]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
6cy6 is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.75Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
ATDA_ECOLI Regulates polyamine concentration by their degradation. Acts on spermidine, forming N(1)- and N(8)-acetylspermidine.
Publication Abstract from PubMed
Spermidine N-acetyltransferase (SpeG) transfers an acetyl group from acetyl-coenzyme A to an N-terminal amino group of intracellular spermidine. This acetylation inactivates spermidine, reducing the polyamine toxicity that tends to occur under certain chemical and physical stresses. The structure of the SpeG protein from Vibrio cholerae has been characterized: while the monomer possesses a structural fold similar to those of other Gcn5-related N-acetyltransferase superfamily members, its dodecameric structure remains exceptional. In this paper, structural analyses of SpeG isolated from Escherichia coli are described. Like V. cholerae SpeG, E. coli SpeG forms dodecamers, as revealed by two crystal structures of the ligand-free E. coli SpeG dodecamer determined at 1.75 and 2.9 A resolution. Although both V. cholerae SpeG and E. coli SpeG can adopt an asymmetric open dodecameric state, solution analysis showed that the oligomeric composition of ligand-free E. coli SpeG differs from that of ligand-free V. cholerae SpeG. Based on these data, it is proposed that the equilibrium balance of SpeG oligomers in the absence of ligands differs from one species to another and thus might be important for SpeG function.
Analysis of crystalline and solution states of ligand-free spermidine N-acetyltransferase (SpeG) from Escherichia coli.,Filippova EV, Weigand S, Kiryukhina O, Wolfe AJ, Anderson WF Acta Crystallogr D Struct Biol. 2019 Jun 1;75(Pt 6):545-553. doi:, 10.1107/S2059798319006545. Epub 2019 May 28. PMID:31205017[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Filippova EV, Weigand S, Kiryukhina O, Wolfe AJ, Anderson WF. Analysis of crystalline and solution states of ligand-free spermidine N-acetyltransferase (SpeG) from Escherichia coli. Acta Crystallogr D Struct Biol. 2019 Jun 1;75(Pt 6):545-553. doi:, 10.1107/S2059798319006545. Epub 2019 May 28. PMID:31205017 doi:http://dx.doi.org/10.1107/S2059798319006545
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