|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4r9m' size='340' side='right'caption='[[4r9m]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='4r9m' size='340' side='right'caption='[[4r9m]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4r9m]] is a 3 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=4R9M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R9M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4r9m]] is a 3 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=4R9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R9M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1584, JW1576, speG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4r9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r9m OCA], [https://pdbe.org/4r9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r9m RCSB], [https://www.ebi.ac.uk/pdbsum/4r9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r9m ProSAT]</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=4r9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r9m OCA], [http://pdbe.org/4r9m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r9m RCSB], [http://www.ebi.ac.uk/pdbsum/4r9m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r9m 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 == |
| Line 27: |
Line 25: |
| | __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: Grimshaw S]] |
| - | [[Category: Grimshaw, S]] | + | [[Category: Kiryukhina O]] |
| - | [[Category: Kiryukhina, O]] | + | [[Category: Minasov G]] |
| - | [[Category: Minasov, G]] | + | [[Category: Shuvalova L]] |
| - | [[Category: Shuvalova, L]] | + | [[Category: Wolfe AJ]] |
| - | [[Category: Wolfe, A J]] | + | |
| - | [[Category: Csgid]]
| + | |
| - | [[Category: National institute of allergy and infectious disease]]
| + | |
| - | [[Category: Niaid]]
| + | |
| - | [[Category: Spermidine/spermine]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
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
|
