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| | <StructureSection load='4k9s' size='340' side='right'caption='[[4k9s]], [[Resolution|resolution]] 2.33Å' scene=''> | | <StructureSection load='4k9s' size='340' side='right'caption='[[4k9s]], [[Resolution|resolution]] 2.33Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4k9s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neisseria_meningitidis_4119 Neisseria meningitidis 4119]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K9S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K9S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4k9s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_4119 Neisseria meningitidis 4119]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K9S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K9S FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4k3u|4k3u]], [[4k40|4k40]], [[4k7j|4k7j]]</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=4k9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k9s OCA], [https://pdbe.org/4k9s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k9s RCSB], [https://www.ebi.ac.uk/pdbsum/4k9s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k9s ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Neisseria meningitidis, NM4119_1198 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1095679 Neisseria meningitidis 4119])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k9s OCA], [http://pdbe.org/4k9s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k9s RCSB], [http://www.ebi.ac.uk/pdbsum/4k9s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k9s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Neisseria meningitidis 4119]] | | [[Category: Neisseria meningitidis 4119]] |
| - | [[Category: Boneca, I Gompert]] | + | [[Category: Gompert Boneca I]] |
| - | [[Category: Williams, A H]] | + | [[Category: Williams AH]] |
| - | [[Category: Alpha/beta fold]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Peptidoglycan hydrolase]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Peptidoglycan O-acetylesterase (Ape1), which is required for host survival in Neisseria sp., belongs to the diverse SGNH hydrolase superfamily, which includes important viral and bacterial virulence factors. Here, multi-domain crystal structures of Ape1 with an SGNH catalytic domain and a newly identified putative peptidoglycan-detection module are reported. Enzyme catalysis was performed in Ape1 crystals and key catalytic intermediates along the SGNH esterase hydrolysis reaction pathway were visualized, revealing a substrate-induced productive conformation of the catalytic triad, a mechanistic detail that has not previously been observed. This substrate-induced productive conformation of the catalytic triad shifts the established dogma on these enzymes, generating valuable insight into the structure-based design of drugs targeting the SGNH esterase superfamily.
Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members.,Williams AH, Veyrier FJ, Bonis M, Michaud Y, Raynal B, Taha MK, White SW, Haouz A, Boneca IG Acta Crystallogr D Biol Crystallogr. 2014 Oct 1;70(Pt 10):2631-9. doi:, 10.1107/S1399004714016770. Epub 2014 Sep 27. PMID:25286847[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Williams AH, Veyrier FJ, Bonis M, Michaud Y, Raynal B, Taha MK, White SW, Haouz A, Boneca IG. Visualization of a substrate-induced productive conformation of the catalytic triad of the Neisseria meningitidis peptidoglycan O-acetylesterase reveals mechanistic conservation in SGNH esterase family members. Acta Crystallogr D Biol Crystallogr. 2014 Oct 1;70(Pt 10):2631-9. doi:, 10.1107/S1399004714016770. Epub 2014 Sep 27. PMID:25286847 doi:http://dx.doi.org/10.1107/S1399004714016770
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