View source for 4mkj


==Crystal structure of L-methionine gamma-lyase from Citrobacter freundii modified by allicine==
<StructureSection load='4mkj' size='340' side='right'caption='[[4mkj]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4mkj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_freundii Citrobacter freundii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MKJ 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]] 1.849&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=C1S:3-(PROP-2-EN-1-YLDISULFANYL)-L-ALANINE'>C1S</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></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=4mkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mkj OCA], [https://pdbe.org/4mkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mkj RCSB], [https://www.ebi.ac.uk/pdbsum/4mkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mkj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q84AR1_CITFR Q84AR1_CITFR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The interaction of Citrobacter freundii methionine gamma-lyase (MGL) and the mutant form in which Cys115 is replaced by Ala (MGL C115A) with the nonprotein amino acid (2R)-2-amino-3-[(S)-prop-2-enylsulfinyl]propanoic acid (alliin) was investigated. It was found that MGL catalyzes the beta-elimination reaction of alliin to form 2-propenethiosulfinate (allicin), pyruvate and ammonia. The beta-elimination reaction of alliin is followed by the inactivation and modification of SH groups of the wild-type and mutant enzymes. Three-dimensional structures of inactivated wild-type MGL (iMGL wild type) and a C115A mutant form (iMGL C115A) were determined at 1.85 and 1.45 A resolution and allowed the identification of the SH groups that were oxidized by allicin. On this basis, the mechanism of the inactivation of MGL by alliin, a new suicide substrate of MGL, is proposed.

Alliin is a suicide substrate of Citrobacter freundii methionine gamma-lyase: structural bases of inactivation of the enzyme.,Morozova EA, Revtovich SV, Anufrieva NV, Kulikova VV, Nikulin AD, Demidkina TV Acta Crystallogr D Biol Crystallogr. 2014 Nov;70(Pt 11):3034-42. doi:, 10.1107/S1399004714020938. Epub 2014 Oct 29. PMID:25372692<ref>PMID:25372692</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4mkj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Methionine gamma-lyase 3D structures|Methionine gamma-lyase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Citrobacter freundii]]
[[Category: Large Structures]]
[[Category: Demidkina TV]]
[[Category: Morozova EA]]
[[Category: Nikulin AD]]
[[Category: Revtovich SV]]
[[Category: Zakomirdina LN]]