View source for 2n58


==Structure of an N-terminal membrane-anchoring region of the glycosyltransferase WaaG==
<StructureSection load='2n58' size='340' side='right'caption='[[2n58]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2n58]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N58 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2n58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n58 OCA], [https://pdbe.org/2n58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n58 RCSB], [https://www.ebi.ac.uk/pdbsum/2n58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n58 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RFAG_ECOLI RFAG_ECOLI] Involved in the addition of the first glucose residue to the lipopolysaccharide core.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The glycosyltransferase WaaG is involved in the synthesis of lipopolysaccharides that constitute the outer leaflet of the outer membrane in Gram-negative bacteria such as Escherichia coli. WaaG has been identified as a potential antibiotic target, and inhibitor scaffolds have previously been investigated. WaaG is located at the cytosolic side of the inner membrane, where the enzyme catalyzes the transfer of the first outer-core glucose to the inner core of nascent lipopolysaccharides. Here, we characterized the binding of WaaG to membrane models designed to mimic the inner membrane of E. coli. Based on the crystal structure, we identified an exposed and largely alpha-helical 30-residue sequence, with a net positive charge and several aromatic amino acids, as a putative membrane-interacting region of WaaG (MIR-WaaG). We studied the peptide corresponding to this sequence, along with its bilayer interactions, using circular dichroism, fluorescence quenching, fluorescence anisotropy, and NMR. In the presence of dodecylphosphocholine, MIR-WaaG was observed to adopt a three-dimensional structure remarkably similar to the segment in the crystal structure. We found that the membrane interaction of WaaG is conferred at least in part by MIR-WaaG and that electrostatic interactions play a key role in binding. Moreover, we propose a mechanism of anchoring WaaG to the inner membrane of E. coli, where the central part of MIR-WaaG inserts into one leaflet of the bilayer. In this model, electrostatic interactions as well as surface-exposed Tyr residues bind WaaG to the membrane.

Membrane Interaction of the Glycosyltransferase WaaG.,Liebau J, Pettersson P, Szpryngiel S, Maler L Biophys J. 2015 Aug 4;109(3):552-63. doi: 10.1016/j.bpj.2015.06.036. PMID:26244737<ref>PMID:26244737</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2n58" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Liebau J]]
[[Category: Maler L]]
[[Category: Pettersson P]]
[[Category: Szpryngiel S]]