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4k40
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Peptidoglycan O-acetylesterase in action, 0 min== | |
| + | <StructureSection load='4k40' size='340' side='right'caption='[[4k40]], [[Resolution|resolution]] 2.63Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4k40]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_LNP21362 Neisseria meningitidis LNP21362]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K40 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=4k40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k40 OCA], [https://pdbe.org/4k40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k40 RCSB], [https://www.ebi.ac.uk/pdbsum/4k40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k40 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0A8F713_NEIME A0A0A8F713_NEIME] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:25286847</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4k40" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Neisseria meningitidis LNP21362]] | ||
| + | [[Category: Gompert Boneca I]] | ||
| + | [[Category: Williams AH]] | ||
Current revision
Peptidoglycan O-acetylesterase in action, 0 min
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