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| | <StructureSection load='6cf9' size='340' side='right'caption='[[6cf9]], [[Resolution|resolution]] 2.29Å' scene=''> | | <StructureSection load='6cf9' size='340' side='right'caption='[[6cf9]], [[Resolution|resolution]] 2.29Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6cf9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CF9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6CF9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6cf9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Campylobacter_jejuni Campylobacter jejuni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CF9 FirstGlance]. <br> |
| - | </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=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.29Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6cf8|6cf8]]</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=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6cf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cf9 OCA], [http://pdbe.org/6cf9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cf9 RCSB], [http://www.ebi.ac.uk/pdbsum/6cf9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cf9 ProSAT]</span></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=6cf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cf9 OCA], [https://pdbe.org/6cf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cf9 RCSB], [https://www.ebi.ac.uk/pdbsum/6cf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cf9 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Campylobacter jejuni]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Akker, F van den]]
| + | [[Category: Kumar V]] |
| - | [[Category: Kumar, V]] | + | [[Category: Van den Akker F]] |
| - | [[Category: Hydrolase]] | + | |
| Structural highlights
Publication Abstract from PubMed
The bacterial soluble lytic transglycosylase (LT) breaks down the peptidoglycan (PG) layer during processes such as cell division. We present here crystal structures of the soluble LT Cj0843 from Campylobacter jejuni with and without bulgecin A inhibitor in the active site. Cj0843 has a doughnut shape similar but not identical to that of E. coli SLT70. The C-terminal catalytic domain is preceded by an L-domain, a large helical U-domain, a flexible linker, and a small N-terminal NU-domain. The flexible linker allows the NU-domain to reach over and complete the circular shape, using residues conserved in the Epsilonproteobacteria LT family. The inner surface of the Cj0843 doughnut is mostly positively charged including a pocket that has 8 Arg/Lys residues. Molecular dynamics simulations with PG strands revealed a potential functional role for this pocket in anchoring the negatively charged terminal tetrapeptide of the PG during several steps in the reaction including homing and aligning the PG strand for exolytic cleavage, and subsequent ratcheting of the PG strand to enhance processivity in degrading PG strands.
Structural studies and molecular dynamics simulations suggest a processive mechanism of exolytic lytic transglycosylase from Campylobacter jejuni.,Vijayaraghavan J, Kumar V, Krishnan NP, Kaufhold RT, Zeng X, Lin J, van den Akker F PLoS One. 2018 May 14;13(5):e0197136. doi: 10.1371/journal.pone.0197136., eCollection 2018. PMID:29758058[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vijayaraghavan J, Kumar V, Krishnan NP, Kaufhold RT, Zeng X, Lin J, van den Akker F. Structural studies and molecular dynamics simulations suggest a processive mechanism of exolytic lytic transglycosylase from Campylobacter jejuni. PLoS One. 2018 May 14;13(5):e0197136. doi: 10.1371/journal.pone.0197136., eCollection 2018. PMID:29758058 doi:http://dx.doi.org/10.1371/journal.pone.0197136
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