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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]] 1.45&Aring;' scene=''>
<StructureSection load='4mkk' size='340' side='right'caption='[[4mkk]], [[Resolution|resolution]] 1.45&Aring;' 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MKK FirstGlance]. <br>
<table><tr><td colspan='2'>[[4mkk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_freundii"_braak_1928 "bacterium freundii" braak 1928]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MKK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rfv|2rfv]], [[4mkj|4mkj]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rfv|2rfv]], [[4mkj|4mkj]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">megL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=546 "Bacterium freundii" Braak 1928])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_gamma-lyase Methionine gamma-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.11 4.4.1.11] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_gamma-lyase Methionine gamma-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.11 4.4.1.11] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mkk OCA], [http://pdbe.org/4mkk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mkk RCSB], [http://www.ebi.ac.uk/pdbsum/4mkk PDBsum], [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mkk OCA], [http://pdbe.org/4mkk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mkk RCSB], [http://www.ebi.ac.uk/pdbsum/4mkk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mkk ProSAT]</span></td></tr>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacterium freundii braak 1928]]
[[Category: Large Structures]]
[[Category: Methionine gamma-lyase]]
[[Category: Methionine gamma-lyase]]
[[Category: Demidkina, T V]]
[[Category: Demidkina, T V]]

Revision as of 11:23, 10 April 2019

Crystal structure of C115A mutant L-methionine gamma-lyase from Citrobacter freundii modified by allicineCrystal structure of C115A mutant L-methionine gamma-lyase from Citrobacter freundii modified by allicine

Structural highlights

4mkk is a 1 chain structure with sequence from "bacterium_freundii"_braak_1928 "bacterium freundii" braak 1928. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
NonStd Res:,
Gene:megL ("Bacterium freundii" Braak 1928)
Activity:Methionine gamma-lyase, with EC number 4.4.1.11
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

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

4mkk, resolution 1.45Å

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