View source for 4qc2


==Crystal structure of lipopolysaccharide transport protein LptB in complex with ATP and Magnesium ions==
<StructureSection load='4qc2' size='340' side='right'caption='[[4qc2]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4qc2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_DH1 Escherichia coli DH1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QC2 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]] 2.22&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4qc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qc2 OCA], [https://pdbe.org/4qc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qc2 RCSB], [https://www.ebi.ac.uk/pdbsum/4qc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qc2 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lipopolysaccharide (LPS) is the main component of the outer membrane of Gram-negative bacteria, which plays an essential role in protecting the bacteria from harsh conditions and antibiotics. LPS molecules are transported from the inner membrane to the outer membrane by seven LPS transport proteins. LptB is vital in hydrolyzing ATP to provide energy for LPS transport, however this mechanism is not very clear. Here we report wild-type LptB crystal structure in complex with ATP and Mg(2+), which reveals that its structure is conserved with other nucleotide-binding proteins (NBD). Structural, functional and electron microscopic studies demonstrated that the ATP binding residues, including K42 and T43, are crucial for LptB's ATPase activity, LPS transport and the vitality of Escherichia coli cells with the exceptions of H195A and Q85A; the H195A mutation does not lower its ATPase activity but impairs LPS transport, and Q85A does not alter ATPase activity but causes cell death. Our data also suggest that two protomers of LptB have to work together for ATP hydrolysis and LPS transport. These results have significant impacts in understanding the LPS transport mechanism and developing new antibiotics.

Structural and functional studies of conserved nucleotide-binding protein LptB in lipopolysaccharide transport.,Wang Z, Xiang Q, Zhu X, Dong H, He C, Wang H, Zhang Y, Wang W, Dong C Biochem Biophys Res Commun. 2014 Sep 26;452(3):443-9. doi:, 10.1016/j.bbrc.2014.08.094. Epub 2014 Aug 27. PMID:25172661<ref>PMID:25172661</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4qc2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli DH1]]
[[Category: Large Structures]]
[[Category: Dong C]]
[[Category: Dong H]]
[[Category: He C]]
[[Category: Wang H]]
[[Category: Wang W]]
[[Category: Wang Z]]
[[Category: Xiang Q]]
[[Category: Zhang Y]]
[[Category: Zhu X]]