View source for 4uoo


==Structure of lipoteichoic acid synthase LtaS from Listeria monocytogenes==
<StructureSection load='4uoo' size='340' side='right'caption='[[4uoo]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4uoo]] is a 5 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=4UOO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UOO 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]] 3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4uoo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uoo OCA], [https://pdbe.org/4uoo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uoo RCSB], [https://www.ebi.ac.uk/pdbsum/4uoo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uoo 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 4uoo" 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]]