3ftt: Difference between revisions
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< | ==Crystal Structure of the galactoside O-acetyltransferase from Staphylococcus aureus== | ||
<StructureSection load='3ftt' size='340' side='right'caption='[[3ftt]], [[Resolution|resolution]] 1.60Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ftt]] is a 1 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=3FTT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FTT FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3ftt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ftt OCA], [https://pdbe.org/3ftt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ftt RCSB], [https://www.ebi.ac.uk/pdbsum/3ftt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ftt ProSAT], [https://www.topsan.org/Proteins/CSGID/3ftt TOPSAN]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ATRF2_STAAC ATRF2_STAAC] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ft/3ftt_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ftt ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3ftt" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Galactoside O-acetyltransferase|Galactoside O-acetyltransferase]] | |||
[[Category: Staphylococcus aureus subsp. aureus | == References == | ||
[[Category: Anderson | <references/> | ||
__TOC__ | |||
[[Category: Chruszcz | </StructureSection> | ||
[[Category: Cui | [[Category: Large Structures]] | ||
[[Category: Cymborowski | [[Category: Staphylococcus aureus subsp. aureus COL]] | ||
[[Category: Knapik | [[Category: Anderson WF]] | ||
[[Category: Minor | [[Category: Chruszcz M]] | ||
[[Category: Savchenko | [[Category: Cui H]] | ||
[[Category: Shumilin | [[Category: Cymborowski M]] | ||
[[Category: Xu | [[Category: Knapik AA]] | ||
[[Category: Zimmerman | [[Category: Minor W]] | ||
[[Category: Savchenko A]] | |||
[[Category: Shumilin IA]] | |||
[[Category: Xu X]] | |||
[[Category: Zimmerman MD]] | |||
Latest revision as of 12:52, 6 November 2024
Crystal Structure of the galactoside O-acetyltransferase from Staphylococcus aureusCrystal Structure of the galactoside O-acetyltransferase from Staphylococcus aureus
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMethicillin-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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