2w5t: Difference between revisions

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-{{Seed}}
-[[Image:2w5t.png|left|200px]]
-<!--
+==Structure-based mechanism of lipoteichoic acid synthesis by Staphylococcus aureus LtaS.==
-The line below this paragraph, containing "STRUCTURE_2w5t", creates the "Structure Box" on the page.
+<StructureSection load='2w5t' size='340' side='right'caption='[[2w5t]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2w5t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W5T FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GP9:(2R)-2,3-DIHYDROXYPROPYL+PHOSPHATE'>GP9</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-{{STRUCTURE_2w5t|  PDB=2w5t  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2w5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w5t OCA], [https://pdbe.org/2w5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w5t RCSB], [https://www.ebi.ac.uk/pdbsum/2w5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w5t ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LTAS_STAAW LTAS_STAAW] Catalyzes the polymerization of lipoteichoic acid (LTA) polyglycerol phosphate, a reaction that presumably uses phosphatidylglycerol (PG) as substrate. Is required for staphylococcal growth and cell division process (By similarity).
+== 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/w5/2w5t_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=2w5t ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Staphylococcus aureus synthesizes polyglycerol-phosphate lipoteichoic acid (LTA) from phosphatidylglycerol. LtaS, a predicted membrane protein with 5 N-terminal transmembrane helices followed by a large extracellular part (eLtaS), is required for staphylococcal growth and LTA synthesis. Here, we report the first crystal structure of the eLtaS domain at 1.2-A resolution and show that it assumes a sulfatase-like fold with an alpha/beta core and a C-terminal part composed of 4 anti-parallel beta-strands and a long alpha-helix. Overlaying eLtaS with sulfatase structures identified active site residues, which were confirmed by alanine substitution mutagenesis and in vivo enzyme function assays. The cocrystal structure with glycerol-phosphate and the coordination of a Mn(2+) cation allowed us to propose a reaction mechanism, whereby the active site threonine of LtaS functions as nucleophile for phosphatidylglycerol hydrolysis and formation of a covalent threonine-glycerolphosphate intermediate. These results will aid in the development of LtaS-specific inhibitors for S. aureus and many other Gram-positive pathogens.
-===STRUCTURE-BASED MECHANISM OF LIPOTEICHOIC ACID SYNTHESIS BY STAPHYLOCOCCUS AUREUS LTAS.===
+Structure-based mechanism of lipoteichoic acid synthesis by Staphylococcus aureus LtaS.,Lu D, Wormann ME, Zhang X, Schneewind O, Grundling A, Freemont PS Proc Natl Acad Sci U S A. 2009 Jan 23. PMID:19168632<ref>PMID:19168632</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_19168632}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2w5t" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 19168632 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19168632}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-W5T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W5T OCA].
-==Reference==
-Structure-based mechanism of lipoteichoic acid synthesis by Staphylococcus aureus LtaS., Lu D, Wormann ME, Zhang X, Schneewind O, Grundling A, Freemont PS, Proc Natl Acad Sci U S A. 2009 Jan 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/19168632 19168632]
-[[Category: Single protein]]
 [[Category: Staphylococcus aureus]]
-[[Category: Pdbx_ordinal=, <PDBx:audit_author.]]
+[[Category: Freemont PS]]
-[[Category: Cell membrane]]
+[[Category: Grundling A]]
-[[Category: Cell wall biogenesis/degradation]]
+[[Category: Lu D]]
-[[Category: Glycerol-phosphate]]
+[[Category: Schneewind O]]
-[[Category: Lta]]
+[[Category: Wormann ME]]
-[[Category: Membrane]]
+[[Category: Zhang X]]
-[[Category: Secreted]]
-[[Category: Transferase]]
-[[Category: Transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 20:11:14 2009''