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==Crystal structure of Campylobacter jejuni Cj0843c lytic transglycosylase in complex with N,N',N''-triacetylchitotriose== | ==Crystal structure of Campylobacter jejuni Cj0843c lytic transglycosylase in complex with N,N',N''-triacetylchitotriose== | ||
<StructureSection load='7lam' size='340' side='right'caption='[[7lam]]' scene=''> | <StructureSection load='7lam' size='340' side='right'caption='[[7lam]], [[Resolution|resolution]] 2.31Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LAM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LAM FirstGlance]. <br> | <table><tr><td colspan='2'>[[7lam]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LAM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LAM FirstGlance]. <br> | ||
</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=7lam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lam OCA], [https://pdbe.org/7lam PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lam RCSB], [https://www.ebi.ac.uk/pdbsum/7lam PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lam ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=7lam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lam OCA], [https://pdbe.org/7lam PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lam RCSB], [https://www.ebi.ac.uk/pdbsum/7lam PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lam ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The soluble lytic transglycosylase Cj0843c from Campylobacter jejuni breaks down cell-wall peptidoglycan (PG). Its nonhydrolytic activity sustains cell-wall remodeling and repair. We report herein our structure-function studies probing the substrate preferences and recognition by this enzyme. Our studies show that Cj0843c exhibits both exolytic and endolytic activities and forms the N-acetyl-1,6-anhydromuramyl (anhMurNAc) peptidoglycan termini, the typical transformation catalyzed by lytic transglycosylase. Cj0843c shows a trend toward a preference for substrates with anhMurNAc ends and those with peptide stems. Mutagenesis revealed that the catalytic E390 is critical for activity. In addition, mutagenesis showed that R388 and K505, located in the positively charged pocket near E390, also serve important roles. Mutation of R326, on the opposite side of this positively charged pocket, enhanced activity. Our data point to different roles for positively charged residues in this pocket for productive binding of the predominantly negatively charged PG. We also show by X-ray crystallography and by molecular dynamics simulations that the active site of Cj0843c is still capable of binding GlcNAc containing di- and trisaccharides without MurNAc moieties, without peptide stems, and without the anhMurNAc ends. | |||
Turnover Chemistry and Structural Characterization of the Cj0843c Lytic Transglycosylase of Campylobacter jejuni.,Kumar V, Mathure SA, Lee M, Boorman J, Zeng X, Lin J, Hesek D, Lastochkin E, Mobashery S, van den Akker F Biochemistry. 2021 Apr 13;60(14):1133-1144. doi: 10.1021/acs.biochem.1c00027., Epub 2021 Mar 22. PMID:33749238<ref>PMID:33749238</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7lam" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kumar V]] | [[Category: Akker, F van den]] | ||
[[Category: | [[Category: Kumar, V]] | ||
[[Category: Complex]] | |||
[[Category: Inhibitor]] | |||
[[Category: Lyase]] | |||
[[Category: Lyase-lyase inhibitor complex]] | |||
[[Category: Substrate analog]] | |||
Revision as of 08:34, 28 April 2021
Crystal structure of Campylobacter jejuni Cj0843c lytic transglycosylase in complex with N,N',N-triacetylchitotrioseCrystal structure of Campylobacter jejuni Cj0843c lytic transglycosylase in complex with N,N',N-triacetylchitotriose
Structural highlights
Publication Abstract from PubMedThe soluble lytic transglycosylase Cj0843c from Campylobacter jejuni breaks down cell-wall peptidoglycan (PG). Its nonhydrolytic activity sustains cell-wall remodeling and repair. We report herein our structure-function studies probing the substrate preferences and recognition by this enzyme. Our studies show that Cj0843c exhibits both exolytic and endolytic activities and forms the N-acetyl-1,6-anhydromuramyl (anhMurNAc) peptidoglycan termini, the typical transformation catalyzed by lytic transglycosylase. Cj0843c shows a trend toward a preference for substrates with anhMurNAc ends and those with peptide stems. Mutagenesis revealed that the catalytic E390 is critical for activity. In addition, mutagenesis showed that R388 and K505, located in the positively charged pocket near E390, also serve important roles. Mutation of R326, on the opposite side of this positively charged pocket, enhanced activity. Our data point to different roles for positively charged residues in this pocket for productive binding of the predominantly negatively charged PG. We also show by X-ray crystallography and by molecular dynamics simulations that the active site of Cj0843c is still capable of binding GlcNAc containing di- and trisaccharides without MurNAc moieties, without peptide stems, and without the anhMurNAc ends. Turnover Chemistry and Structural Characterization of the Cj0843c Lytic Transglycosylase of Campylobacter jejuni.,Kumar V, Mathure SA, Lee M, Boorman J, Zeng X, Lin J, Hesek D, Lastochkin E, Mobashery S, van den Akker F Biochemistry. 2021 Apr 13;60(14):1133-1144. doi: 10.1021/acs.biochem.1c00027., Epub 2021 Mar 22. PMID:33749238[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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