View source for 5vgl


==Crystal structure of lachrymatory factor synthase from Allium cepa==
<StructureSection load='5vgl' size='340' side='right'caption='[[5vgl]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vgl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Allium_cepa Allium cepa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VGL 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]] 1.4&#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=5vgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vgl OCA], [https://pdbe.org/5vgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vgl RCSB], [https://www.ebi.ac.uk/pdbsum/5vgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vgl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LFS_ALLCE LFS_ALLCE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The biochemical pathway that gives onions their savor is part of the chemical warfare against microbes and animals. This defense mechanism involves formation of a volatile lachrymatory factor (LF) ((Z)-propanethial S-oxide) that causes familiar eye irritation associated with onion chopping. LF is produced in a reaction catalyzed by lachrymatory factor synthase (LFS). The principles by which LFS facilitates conversion of a sulfenic acid substrate into LF have been difficult to experimentally examine owing to the inherent substrate reactivity and lability of LF. To shed light on the mechanism of LF production in the onion, we solved crystal structures of LFS in an apo-form and in complex with a substrate analogue, crotyl alcohol. The enzyme closely resembles the helix-grip fold characteristic for plant representatives of the START (star-related lipid transfer) domain-containing protein superfamily. By comparing the structures of LFS to that of the abscisic acid receptor, PYL10, a representative of the START protein superfamily, we elucidated structural adaptations underlying the catalytic activity of LFS. We also delineated the architecture of the active site, and based on the orientation of the ligand, we propose a mechanism of catalysis that involves sequential proton transfer accompanied by formation of a carbanion intermediate. These findings reconcile chemical and biochemical information regarding thioaldehyde S-oxide formation and close a long-lasting gap in understanding of the mechanism responsible for LF production in the onion.

Enzyme That Makes You Cry-Crystal Structure of Lachrymatory Factor Synthase from Allium cepa.,Silvaroli JA, Pleshinger MJ, Banerjee S, Kiser PD, Golczak M ACS Chem Biol. 2017 Jul 26. doi: 10.1021/acschembio.7b00336. PMID:28708375<ref>PMID:28708375</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vgl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Allium cepa]]
[[Category: Large Structures]]
[[Category: Banerjee S]]
[[Category: Golczak M]]
[[Category: Kiser PD]]
[[Category: Pleshinger MJ]]
[[Category: Silvaroli JA]]