3v4e: Difference between revisions

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 ==Crystal Structure of the galactoside O-acetyltransferase in complex with CoA==
-<StructureSection load='3v4e' size='340' side='right' caption='[[3v4e]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+<StructureSection load='3v4e' size='340' side='right'caption='[[3v4e]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3v4e]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Staac Staac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3V4E FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3v4e]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_COL Staphylococcus aureus subsp. aureus COL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V4E 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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.95&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ftt|3ftt]]</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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SACOL2570 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93062 STAAC])</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=3v4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v4e OCA], [https://pdbe.org/3v4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v4e RCSB], [https://www.ebi.ac.uk/pdbsum/3v4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v4e 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=3v4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v4e OCA], [http://pdbe.org/3v4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3v4e RCSB], [http://www.ebi.ac.uk/pdbsum/3v4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3v4e ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/ATRF2_STAAC ATRF2_STAAC]
-Methicillin-resistant Staphylococcus aureus (MRSA) is a major cause of a myriad of insidious and intractable infections in humans, especially in patients with compromised immune systems and children. Here, we report the apo- and CoA-bound crystal structures of a member of the galactoside acetyltransferase superfamily from methicillin-resistant S. aureus SACOL2570 which was recently shown to be down regulated in S. aureus grown in the presence of fusidic acid, an antibiotic used to treat MRSA infections. SACOL2570 forms a homotrimer in solution, as confirmed by small-angle X-ray scattering and dynamic light scattering. The protein subunit consists of an N-terminal alpha-helical domain connected to a C-terminal LbetaH domain. CoA binds in the active site formed by the residues from adjacent LbetaH domains. After determination of CoA-bound structure, molecular dynamics simulations were performed to model the binding of AcCoA. Binding of both AcCoA and CoA to SACOL2570 was verified by isothermal titration calorimetry. SACOL2570 most likely acts as an acetyltransferase, using AcCoA as an acetyl group donor and an as-yet-undetermined chemical moiety as an acceptor. SACOL2570 was recently used as a scaffold for mutations that lead the generation of cage-like assemblies, and has the potential to be used for the generation of more complex nanostructures.
-Biophysical analysis of the putative acetyltransferase SACOL2570 from methicillin-resistant Staphylococcus aureus.,Luo HB, Knapik AA, Petkowski JJ, Demas M, Shumilin IA, Zheng H, Chruszcz M, Minor W J Struct Funct Genomics. 2013 Sep;14(3):97-108. doi: 10.1007/s10969-013-9158-6., Epub 2013 Aug 21. PMID:23963951<ref>PMID:23963951</ref>
+==See Also==
+*[[Galactoside O-acetyltransferase|Galactoside O-acetyltransferase]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3v4e" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Staac]]
+[[Category: Large Structures]]
-[[Category: Anderson, W F]]
+[[Category: Staphylococcus aureus subsp. aureus COL]]
-[[Category: Structural genomic]]
+[[Category: Anderson WF]]
-[[Category: Chruszcz, M]]
+[[Category: Chruszcz M]]
-[[Category: Cymborowski, M]]
+[[Category: Cymborowski M]]
-[[Category: Knapik, A A]]
+[[Category: Knapik AA]]
-[[Category: Luo, H B]]
+[[Category: Luo H-B]]
-[[Category: Minor, W]]
+[[Category: Minor W]]
-[[Category: Shumilin, I A]]
+[[Category: Shumilin IA]]
-[[Category: Zimmerman, M D]]
+[[Category: Zimmerman MD]]
-[[Category: Coa]]
-[[Category: Csgid]]
-[[Category: Galactoside o-acetyltransferase]]
-[[Category: Transferase]]