4uop: Difference between revisions
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New page: '''Unreleased structure''' The entry 4uop is ON HOLD until Paper Publication Authors: Campeotto, I., Freemont, P., Grundling, A. Description: Crystal structure of the lipoteichoic acid... |
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==Crystal structure of the lipoteichoic acid synthase LtaP from Listeria monocytogenes== | |||
<StructureSection load='4uop' size='340' side='right'caption='[[4uop]], [[Resolution|resolution]] 1.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4uop]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UOP 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]] 1.75Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4uop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uop OCA], [https://pdbe.org/4uop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uop RCSB], [https://www.ebi.ac.uk/pdbsum/4uop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uop ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8Y989_LISMO Q8Y989_LISMO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Lipoteichoic acid (LTA) is an important cell wall component required for proper cell growth in many Gram-positive bacteria. In Listeria monocytogenes, two enzymes are required for the synthesis of this polyglycerolphosphate polymer. The LTA primase LtaPLm initiates LTA synthesis by transferring the first glycerolphosphate (GroP) subunit onto the glycolipid anchor and the LTA synthase LtaSLm extends the polymer by the repeated addition of GroP subunits to the tip of the growing chain. Here, we present the crystal structures of the enzymatic domains of LtaPLm and LtaSLm. While the enzymes share the same fold, substantial differences in the cavity of the catalytic site and surface charge distribution contribute to enzyme specialization. The eLtaSLm structure was also determined in complex with GroP revealing a second GroP binding site. Mutational analysis confirmed an essential function for this binding site and allowed us to propose a model for the binding of the growing chain. | |||
Structural and Mechanistic Insight into the Listeria monocytogenes Two-Enzyme Lipoteichoic Acid Synthesis System.,Campeotto I, Percy MG, MacDonald JT, Forster A, Freemont PS, Grundling A J Biol Chem. 2014 Aug 15. pii: jbc.M114.590570. PMID:25128528<ref>PMID:25128528</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4uop" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Listeria monocytogenes EGD-e]] | |||
[[Category: Campeotto I]] | |||
[[Category: Freemont P]] | |||
[[Category: Grundling A]] | |||
Latest revision as of 10:32, 10 January 2024
Crystal structure of the lipoteichoic acid synthase LtaP from Listeria monocytogenes
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