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| | <StructureSection load='4k3u' size='340' side='right'caption='[[4k3u]], [[Resolution|resolution]] 2.16Å' scene=''> | | <StructureSection load='4k3u' size='340' side='right'caption='[[4k3u]], [[Resolution|resolution]] 2.16Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4k3u]] 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=4K3U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K3U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4k3u]] 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=4K3U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K3U FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</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]] 2.158Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></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=4k3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k3u OCA], [http://pdbe.org/4k3u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k3u RCSB], [http://www.ebi.ac.uk/pdbsum/4k3u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k3u 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=4k3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k3u OCA], [https://pdbe.org/4k3u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k3u RCSB], [https://www.ebi.ac.uk/pdbsum/4k3u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k3u 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 Gomperts]] | + | [[Category: Gomperts Boneca I]] |
| - | [[Category: Williams, A H]] | + | [[Category: Williams AH]] |
| - | [[Category: Alpha/beta fold]]
| + | |
| - | [[Category: Hydrolase]]
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| - | [[Category: Peptidoglycan hydrolase]]
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| 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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