3wr7: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal Structure of Spermidine Acetyltransferase from Escherichia coli== | ==Crystal Structure of Spermidine Acetyltransferase from Escherichia coli== | ||
<StructureSection load='3wr7' size='340' side='right' caption='[[3wr7]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='3wr7' size='340' side='right' caption='[[3wr7]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| Line 4: | Line 5: | ||
<table><tr><td colspan='2'>[[3wr7]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WR7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WR7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3wr7]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WR7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WR7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene></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=3wr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wr7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wr7 RCSB], [http://www.ebi.ac.uk/pdbsum/3wr7 PDBsum]</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=3wr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wr7 OCA], [http://pdbe.org/3wr7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wr7 RCSB], [http://www.ebi.ac.uk/pdbsum/3wr7 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Spermidine acetyltransferase (SAT) from Escherichia coli, which catalyses the transfer of acetyl groups from acetyl-CoA to spermidine, is a key enzyme in controlling polyamine levels in prokaryotic cells. In this study, we determined the crystal structure of SAT in complex with spermidine (SPD) and CoA at 2.5A resolution. SAT is a dodecamer organized as a hexamer of dimers. The secondary structural element and folding topology of the SAT dimer resemble those of spermidine/spermine N(1)-acetyltransferase (SSAT), suggesting an evolutionary link between SAT and SSAT. However, the polyamine specificity of SAT is distinct from that of SSAT and is promiscuous. The SPD molecule is also located at the inter-dimer interface. The distance between SPD and CoA molecules is 13A. A deep, highly acidic, water-filled cavity encompasses the SPD and CoA binding sites. Structure-based mutagenesis and in-vitro assays identified SPD-bound residues, and the acidic residues lining the walls of the cavity are mostly essential for enzymatic activities. Based on mutagenesis and structural data, we propose an acetylation mechanism underlying promiscuous polyamine recognition for SAT. | |||
Molecular mechanism underlying promiscuous polyamine recognition by spermidine acetyltransferase.,Sugiyama S, Ishikawa S, Tomitori H, Niiyama M, Hirose M, Miyazaki Y, Higashi K, Murata M, Adachi H, Takano K, Murakami S, Inoue T, Mori Y, Kashiwagi K, Igarashi K, Matsumura H Int J Biochem Cell Biol. 2016 Jul;76:87-97. doi: 10.1016/j.biocel.2016.05.003., Epub 2016 May 6. PMID:27163532<ref>PMID:27163532</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3wr7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:45, 20 June 2016
Crystal Structure of Spermidine Acetyltransferase from Escherichia coliCrystal Structure of Spermidine Acetyltransferase from Escherichia coli
Structural highlights
Publication Abstract from PubMedSpermidine acetyltransferase (SAT) from Escherichia coli, which catalyses the transfer of acetyl groups from acetyl-CoA to spermidine, is a key enzyme in controlling polyamine levels in prokaryotic cells. In this study, we determined the crystal structure of SAT in complex with spermidine (SPD) and CoA at 2.5A resolution. SAT is a dodecamer organized as a hexamer of dimers. The secondary structural element and folding topology of the SAT dimer resemble those of spermidine/spermine N(1)-acetyltransferase (SSAT), suggesting an evolutionary link between SAT and SSAT. However, the polyamine specificity of SAT is distinct from that of SSAT and is promiscuous. The SPD molecule is also located at the inter-dimer interface. The distance between SPD and CoA molecules is 13A. A deep, highly acidic, water-filled cavity encompasses the SPD and CoA binding sites. Structure-based mutagenesis and in-vitro assays identified SPD-bound residues, and the acidic residues lining the walls of the cavity are mostly essential for enzymatic activities. Based on mutagenesis and structural data, we propose an acetylation mechanism underlying promiscuous polyamine recognition for SAT. Molecular mechanism underlying promiscuous polyamine recognition by spermidine acetyltransferase.,Sugiyama S, Ishikawa S, Tomitori H, Niiyama M, Hirose M, Miyazaki Y, Higashi K, Murata M, Adachi H, Takano K, Murakami S, Inoue T, Mori Y, Kashiwagi K, Igarashi K, Matsumura H Int J Biochem Cell Biol. 2016 Jul;76:87-97. doi: 10.1016/j.biocel.2016.05.003., Epub 2016 May 6. PMID:27163532[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||