View source for 4k40


==Peptidoglycan O-acetylesterase in action, 0 min==
<StructureSection load='4k40' size='340' side='right'caption='[[4k40]], [[Resolution|resolution]] 2.63&Aring;' 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.634&#8491;</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>
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Neisseria meningitidis LNP21362]]
[[Category: Gompert Boneca I]]
[[Category: Williams AH]]