View source for 6bui


==Crystal structure of a membrane protein, crystal form III==
<StructureSection load='6bui' size='340' side='right'caption='[[6bui]], [[Resolution|resolution]] 3.27&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6bui]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_thermophilus Streptococcus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BUI 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]] 3.27&#8491;</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=6bui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bui OCA], [https://pdbe.org/6bui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bui RCSB], [https://www.ebi.ac.uk/pdbsum/6bui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bui ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DLTB_STRT2 DLTB_STRT2] O-acyltransferase that catalyzes D-alanylation of both teichoic acid and lipoteichoic acid (LTA) (PubMed:30283133). D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall (PubMed:30283133). Catalyzes D-alanylation from DltC carrier protein (PubMed:30283133).<ref>PMID:30283133</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Membrane-bound O-acyltransferases (MBOATs) are a superfamily of integral transmembrane enzymes that are found in all kingdoms of life(1). In bacteria, MBOATs modify protective cell-surface polymers. In vertebrates, some MBOAT enzymes-such as acyl-coenzyme A:cholesterol acyltransferase and diacylglycerol acyltransferase 1-are responsible for lipid biosynthesis or phospholipid remodelling(2,3). Other MBOATs, including porcupine, hedgehog acyltransferase and ghrelin acyltransferase, catalyse essential lipid modifications of secreted proteins such as Wnt, hedgehog and ghrelin, respectively(4-10). Although many MBOAT proteins are important drug targets, little is known about their molecular architecture and functional mechanisms. Here we present crystal structures of DltB, an MBOAT responsible for the D-alanylation of cell-wall teichoic acid in Gram-positive bacteria(11-16), both alone and in complex with the D-alanyl donor protein DltC. DltB contains a ring of 11 peripheral transmembrane helices, which shield a highly conserved extracellular structural funnel extending into the middle of the lipid bilayer. The conserved catalytic histidine residue is located at the bottom of this funnel and is connected to the intracellular DltC through a narrow tunnel. Mutation of either the catalytic histidine or the DltC-binding site of DltB abolishes the D-alanylation of lipoteichoic acid and sensitizes the Gram-positive bacterium Bacillus subtilis to cell-wall stress, which suggests cross-membrane catalysis involving the tunnel. Structure-guided sequence comparison among DltB and vertebrate MBOATs reveals a conserved structural core and suggests that MBOATs from different organisms have similar catalytic mechanisms. Our structures provide a template for understanding structure-function relationships in MBOATs and for developing therapeutic MBOAT inhibitors.

Crystal structure of a membrane-bound O-acyltransferase.,Ma D, Wang Z, Merrikh CN, Lang KS, Lu P, Li X, Merrikh H, Rao Z, Xu W Nature. 2018 Oct;562(7726):286-290. doi: 10.1038/s41586-018-0568-2. Epub 2018 Oct, 3. PMID:30283133<ref>PMID:30283133</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6bui" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus thermophilus]]
[[Category: Ma D]]
[[Category: Wang Z]]
[[Category: Xu W]]