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4mkk
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==Crystal structure of C115A mutant L-methionine gamma-lyase from Citrobacter freundii modified by allicine== | ==Crystal structure of C115A mutant L-methionine gamma-lyase from Citrobacter freundii modified by allicine== | ||
| - | <StructureSection load='4mkk' size='340' side='right' caption='[[4mkk]], [[Resolution|resolution]] 1.45Å' scene=''> | + | <StructureSection load='4mkk' size='340' side='right'caption='[[4mkk]], [[Resolution|resolution]] 1.45Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4mkk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MKK OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[4mkk]] 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=4MKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MKK FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C1S:3-(PROP-2-EN-1-YLDISULFANYL)-L-ALANINE'>C1S</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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=4mkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mkk OCA], [https://pdbe.org/4mkk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mkk RCSB], [https://www.ebi.ac.uk/pdbsum/4mkk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mkk ProSAT]</span></td></tr> | |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4mkk" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Methionine gamma-lyase 3D structures|Methionine gamma-lyase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Citrobacter freundii]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Demidkina TV]] |
| - | [[Category: | + | [[Category: Morozova EA]] |
| - | [[Category: | + | [[Category: Nikulin AD]] |
| - | [[Category: | + | [[Category: Revtovich SV]] |
| - | [[Category: | + | [[Category: Zakomirdina LN]] |
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Current revision
Crystal structure of C115A mutant L-methionine gamma-lyase from Citrobacter freundii modified by allicine
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