5o2n
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5o2n is ON HOLD Authors: Williams, A.H., Wheeler, R., Rateau, L., Malosse, C., Rooke, J.C., Hoauz, A., Taha, M.-K., Boneca, I.G. Description: Lytic...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Lytic transglycosylase in action== | |
| + | <StructureSection load='5o2n' size='340' side='right'caption='[[5o2n]], [[Resolution|resolution]] 1.51Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5o2n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O2N 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]] 1.513Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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=5o2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o2n OCA], [https://pdbe.org/5o2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o2n RCSB], [https://www.ebi.ac.uk/pdbsum/5o2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o2n ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q9JXP1_NEIMB Q9JXP1_NEIMB] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Lytic transglycosylases (LTs) are a class of enzymes important for the recycling and metabo-lism of peptidoglycan (PG). LTs cleave the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) in the PG glycan strand, resulting in the concomitant formation of 1,6-anhydro-MurNAc and GlcNAc. No LTs reported to date have utilized chitins as sub-strates, despite the fact that chitins are GlcNAc pol-ymers linked via beta-1,4-glycosidic bonds, which are the known site of chemical activity for LTs. Here, we demonstrate enzymatically that LtgA, a non-canonical, substrate-permissive LT from Neisseria meningitidis, utilizes chitopentaose ((GlcNAc)5) as a substrate to produce three newly identified sugars: 1,6-anhydro-chitobiose, 1,6-anhydro-chitotriose and 1,6-anhydro-chitotetraose. Although LTs have been widely studied, their complex reactions have not previously been visualized in the crystalline state because macromolecular PG is insoluble. Here, we visualized the cleavage of the glycosidic bond and the liberation of GlcNAc-derived residues by LtgA, followed by the synthesis of atypical 1,6-anhydro-GlcNAc derivatives. In addition to the newly identified anhydro-chitin products, we identi-fied trapped intermediates, unpredicted substrate rearrangements, sugar distortions, and a conserved crystallographic water molecule bound to the cata-lytic glutamate of a high-resolution native LT. This study enabled us to propose a revised alternative mechanism for LtgA that could also be applicable to other LTs. Our work contributes to the understand-ing of the mechanisms of LTs in bacterial cell wall biology. | ||
| - | + | A step-by-step in crystallo guide to bond cleavage and 1,6-anhydro sugar product synthesis by a peptidoglycan degrading lytic transglycosylase.,Williams AH, Wheeler R, Rateau L, Malosse C, Chamot-Rooke J, Haouz A, Taha MK, Boneca IG J Biol Chem. 2018 Feb 26. pii: RA117.001095. doi: 10.1074/jbc.RA117.001095. PMID:29483188<ref>PMID:29483188</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5o2n" style="background-color:#fffaf0;"></div> |
| - | + | == References == | |
| - | [[Category: Boneca | + | <references/> |
| - | [[Category: Hoauz | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Neisseria meningitidis]] | |
| - | + | [[Category: Boneca IG]] | |
| + | [[Category: Hoauz A]] | ||
| + | [[Category: Williams AH]] | ||
Current revision
Lytic transglycosylase in action
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