View source for 4uor


==Structure of lipoteichoic acid synthase LtaS from Listeria monocytogenes in complex with glycerol phosphate==
<StructureSection load='4uor' size='340' side='right'caption='[[4uor]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4uor]] is a 11 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=4UOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UOR 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]] 2.194&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GP9:(2R)-2,3-DIHYDROXYPROPYL+PHOSPHATE'>GP9</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=4uor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uor OCA], [https://pdbe.org/4uor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uor RCSB], [https://www.ebi.ac.uk/pdbsum/4uor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uor ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8Y8H6_LISMO Q8Y8H6_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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4uor" 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]]