View source for 6qk4


==Lytic transglycosylase, LtgG, of Burkholderia pseudomallei.==
<StructureSection load='6qk4' size='340' side='right'caption='[[6qk4]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6qk4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei Burkholderia pseudomallei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QK4 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]] 1.73&#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=6qk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qk4 OCA], [https://pdbe.org/6qk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qk4 RCSB], [https://www.ebi.ac.uk/pdbsum/6qk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qk4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q63QH7_BURPS Q63QH7_BURPS] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Burkholderia pseudomallei is the causative agent of the tropical disease melioidosis. Its genome encodes an arsenal of virulence factors that allow it, when required, to switch from a soil dwelling bacterium to a deadly intracellular pathogen. With a high intrinsic resistance to antibiotics and the ability to overcome challenges from the host immune system, there is an increasing requirement for new antibiotics and a greater understanding into the molecular mechanisms of B. pseudomallei virulence and dormancy. The peptidoglycan remodeling enzymes, lytic transglycosylases (Ltgs) are potential targets for such new antibiotics. Ltgs cleave the glycosidic bonds within bacterial peptidoglycan allowing for the insertion of peptidoglycan precursors during cell growth and division, and cell membrane spanning structures such as flagella and secretion systems. Using bioinformatic analysis we have identified 8 putative Ltgs in B. pseudomallei K96243. We aimed to investigate one of these Ltgs, LtgG (BPSL3046) through the generation of deletion mutants and biochemical analysis. We have shown that LtgG is a key contributor to cellular morphology, division, motility and virulence in BALB/c mice. We have determined the crystal structure of LtgG and have identified various amino acids likely to be important in peptidoglycan binding and catalytic activity. Recombinant protein assays and complementation studies using LtgG containing a site directed mutation in aspartate 343, confirmed the essentiality of this amino acid in the function of LtgG.

The lytic transglycosylase, LtgG, controls cell morphology and virulence in Burkholderia pseudomallei.,Jenkins CH, Wallis R, Allcock N, Barnes KB, Richards MI, Auty JM, Galyov EE, Harding SV, Mukamolova GV Sci Rep. 2019 Jul 30;9(1):11060. doi: 10.1038/s41598-019-47483-z. PMID:31363151<ref>PMID:31363151</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6qk4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Burkholderia pseudomallei]]
[[Category: Large Structures]]
[[Category: Allcock N]]
[[Category: Auty JM]]
[[Category: Barnes KB]]
[[Category: Galyov EE]]
[[Category: Harding SV]]
[[Category: Jenkins CH]]
[[Category: Mukamolova GV]]
[[Category: Richards MI]]
[[Category: Wallis R]]