3wr7: Difference between revisions

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 ==Crystal Structure of Spermidine Acetyltransferase from Escherichia coli==
-<StructureSection load='3wr7' size='340' side='right' caption='[[3wr7]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='3wr7' size='340' side='right'caption='[[3wr7]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3wr7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_ly180 Escherichia coli ly180]. 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 with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_LY180 Escherichia coli LY180]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wr7 ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=3wr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wr7 OCA], [https://pdbe.org/3wr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wr7 RCSB], [https://www.ebi.ac.uk/pdbsum/3wr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wr7 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/A0A0M3KKU5_ECOLX A0A0M3KKU5_ECOLX]
-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&reg;/PubMed&reg;, 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__
 </StructureSection>
-[[Category: Escherichia coli ly180]]
+[[Category: Escherichia coli LY180]]
-[[Category: Adachi, H]]
+[[Category: Large Structures]]
-[[Category: Higashi, K]]
+[[Category: Adachi H]]
-[[Category: Hirose, M]]
+[[Category: Higashi K]]
-[[Category: Igarashi, K]]
+[[Category: Hirose M]]
-[[Category: Inoue, T]]
+[[Category: Igarashi K]]
-[[Category: Ishikawa, S]]
+[[Category: Inoue T]]
-[[Category: Kashiwagi, K]]
+[[Category: Ishikawa S]]
-[[Category: Matsumura, H]]
+[[Category: Kashiwagi K]]
-[[Category: Miyazaki, Y]]
+[[Category: Matsumura H]]
-[[Category: Mori, Y]]
+[[Category: Miyazaki Y]]
-[[Category: Murakami, S]]
+[[Category: Mori Y]]
-[[Category: Niiyama, M]]
+[[Category: Murakami S]]
-[[Category: Sugiyama, S]]
+[[Category: Niiyama M]]
-[[Category: Takano, K]]
+[[Category: Sugiyama S]]
-[[Category: Tomitori, S]]
+[[Category: Takano K]]
-[[Category: Alpha and beta]]
+[[Category: Tomitori S]]
-[[Category: Transferase]]