View source for 5knk


==Lipid A secondary acyltransferase LpxM from Acinetobacter baumannii with catalytic residue substitution (E127A)==
<StructureSection load='5knk' size='340' side='right'caption='[[5knk]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5knk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_NIPH_410 Acinetobacter baumannii NIPH 410]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KNK 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]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=11A:UNDECANOIC+ACID'>11A</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5knk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5knk OCA], [https://pdbe.org/5knk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5knk RCSB], [https://www.ebi.ac.uk/pdbsum/5knk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5knk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/S3TFW2_ACIBA S3TFW2_ACIBA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Gram-negative bacteria possess a characteristic outer membrane, of which the lipid A constituent elicits a strong host immune response through the Toll-like receptor 4 complex, and acts as a component of the permeability barrier to prevent uptake of bactericidal compounds. Lipid A species comprise the bulk of the outer leaflet of the outer membrane and are produced through a multistep biosynthetic pathway conserved in most Gram-negative bacteria. The final steps in this pathway involve the secondary acylation of lipid A precursors. These are catalyzed by members of a superfamily of enzymes known as lysophospholipid acyltransferases (LPLATs), which are present in all domains of life and play important roles in diverse biological processes. To date, characterization of this clinically important class of enzymes has been limited by a lack of structural information and the availability of only low-throughput biochemical assays. In this work, we present the structure of the bacterial LPLAT protein LpxM, and we describe a high-throughput, label-free mass spectrometric assay to characterize acyltransferase enzymatic activity. Using our structure and assay, we identify an LPLAT thioesterase activity, and we provide experimental evidence to support an ordered-binding and "reset" mechanistic model for LpxM function. This work enables the interrogation of other bacterial acyltransferases' structure-mechanism relationships, and the assay described herein provides a foundation for quantitatively characterizing the enzymology of any number of clinically relevant LPLAT proteins.

Structure-guided enzymology of the lipid A acyltransferase LpxM reveals a dual activity mechanism.,Dovala D, Rath CM, Hu Q, Sawyer WS, Shia S, Elling RA, Knapp MS, Metzger LE 4th Proc Natl Acad Sci U S A. 2016 Oct 11;113(41):E6064-E6071. Epub 2016 Sep 28. PMID:27681620<ref>PMID:27681620</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5knk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Acinetobacter baumannii NIPH 410]]
[[Category: Large Structures]]
[[Category: Dovala DL]]
[[Category: Hu Q]]
[[Category: Metzger IV LE]]