3dfk: Difference between revisions
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New page: '''Unreleased structure''' The entry 3dfk is ON HOLD Authors: Zou, Y., Brunzelle, J.S., Nair, S.K. Description: Crystal Structures of Lipoglycopeptide Antibiotic Deacetylases: Implicat... |
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The | ==The crystal structure of teicoplanin pseudoaglycone deacetylase Orf2* bound to one of its products decanoic acid== | ||
<StructureSection load='3dfk' size='340' side='right'caption='[[3dfk]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3dfk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinoplanes_teichomyceticus"_parenti_et_al._1978 "actinoplanes teichomyceticus" parenti et al. 1978]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DFK FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DKA:DECANOIC+ACID'>DKA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dff|3dff]], [[3dfi|3dfi]], [[3dfm|3dfm]]</div></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tcp14 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1867 "Actinoplanes teichomyceticus" Parenti et al. 1978])</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=3dfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dfk OCA], [https://pdbe.org/3dfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dfk RCSB], [https://www.ebi.ac.uk/pdbsum/3dfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dfk ProSAT]</span></td></tr> | |||
</table> | |||
== 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/df/3dfk_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3dfk ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The lipoglycopeptide antibiotics teicoplanin and A40926 have proven efficacy against Gram-positive pathogens. These drugs are distinguished from glycopeptide antibiotics by N-linked long chain acyl-D-glucosamine decorations that contribute to antibacterial efficacy. During the biosynthesis of lipoglycopeptides, tailoring glycosyltransferases attach an N-acetyl-D-glucosamine to the aglycone, and this N-acetyl-glucosaminyl pseudoaglycone is deacetylated prior to long chain hydrocarbon attachment. Here we present several high-resolution crystal structures of the pseudoaglycone deacetylases from the biosynthetic pathways of teicoplanin and A40926. The cocrystal structure of the teicoplanin pseudoaglycone deacetylase with a fatty acid product provides further insights into the roles of active-site residues, and suggests mechanistic similarities with structurally distinct zinc deacetylases, such as peptidoglycan deacetylase and LpxC. A unique, structurally mobile capping lid, located at the apex of these pseudoaglycone deacetylases, likely serves as a determinant of substrate specificity. | |||
Crystal structures of lipoglycopeptide antibiotic deacetylases: implications for the biosynthesis of A40926 and teicoplanin.,Zou Y, Brunzelle JS, Nair SK Chem Biol. 2008 Jun;15(6):533-45. PMID:18559264<ref>PMID:18559264</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3dfk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Actinoplanes teichomyceticus parenti et al. 1978]] | |||
[[Category: Large Structures]] | |||
[[Category: Brunzelle, J S]] | |||
[[Category: Nair, S K]] | |||
[[Category: Zou, Y]] | |||
[[Category: Alpha-beta single domain]] | |||
[[Category: Bound to decanoic acid]] | |||
[[Category: Hydrolase]] | |||
Latest revision as of 07:57, 9 February 2022
The crystal structure of teicoplanin pseudoaglycone deacetylase Orf2* bound to one of its products decanoic acid
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