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| | <StructureSection load='2o7c' size='340' side='right'caption='[[2o7c]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='2o7c' size='340' side='right'caption='[[2o7c]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2o7c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2O7C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2o7c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O7C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O7C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=SO4:SULFATE+ION'>SO4</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=2o7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7c OCA], [https://pdbe.org/2o7c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o7c RCSB], [https://www.ebi.ac.uk/pdbsum/2o7c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7c ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2o7c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o7c OCA], [http://pdbe.org/2o7c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2o7c RCSB], [http://www.ebi.ac.uk/pdbsum/2o7c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2o7c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MEGL_PSEPU MEGL_PSEPU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus fluorescens putidus flugge 1886]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Methionine gamma-lyase]] | + | [[Category: Pseudomonas putida]] |
| - | [[Category: Inagaki, K]] | + | [[Category: Inagaki K]] |
| - | [[Category: Misaki, S]] | + | [[Category: Misaki S]] |
| - | [[Category: Takakura, T]] | + | [[Category: Takakura T]] |
| - | [[Category: Takimoto, A]] | + | [[Category: Takimoto A]] |
| - | [[Category: Tamura, T]] | + | [[Category: Tamura T]] |
| - | [[Category: Tanaka, H]] | + | [[Category: Tanaka H]] |
| - | [[Category: Yamashita, M]] | + | [[Category: Yamashita M]] |
| - | [[Category: Yoshioka, T]] | + | [[Category: Yoshioka T]] |
| - | [[Category: Cancer]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Methionine]]
| + | |
| - | [[Category: Plp]]
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| Structural highlights
Function
MEGL_PSEPU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
l-Methionine gamma-lyase (EC 4.4.1.11, MGL_Pp) from Pseudomonas putida is a multifunctional enzyme, which belongs to the gamma-family of pyridoxal-5'-phosphate (PLP) dependent enzymes. In this report, we demonstrate that the three-dimensional structure of MGL_Pp has been completely solved by the molecular replacement method to an R-factor of 20.4% at 1.8 A resolution. Detailed information of the overall structure of MGL_Pp supplies a clear picture of the substrate- and PLP-binding pockets. Tyr59 and Arg61 of neighbouring subunits, which are strongly conserved in other gamma-family enzymes, contact the phosphate group of PLP. These residues are important as the main anchor within the active site. Lys240, Asp241 and Arg61 of one partner monomer and Tyr114 and Cys116 of the other partner monomer form a hydrogen-bond network in the MGL active site which is specific for MGLs. It is also suggested that electrostatic interactions at the subunit interface are involved in the stabilization of the structural conformation. The detailed structure will facilitate the development of MGL_Pp as an anticancer drug.
Structure of the antitumour enzyme L-methionine gamma-lyase from Pseudomonas putida at 1.8 A resolution.,Kudou D, Misaki S, Yamashita M, Tamura T, Takakura T, Yoshioka T, Yagi S, Hoffman RM, Takimoto A, Esaki N, Inagaki K J Biochem. 2007 Apr;141(4):535-44. Epub 2007 Feb 8. PMID:17289792[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kudou D, Misaki S, Yamashita M, Tamura T, Takakura T, Yoshioka T, Yagi S, Hoffman RM, Takimoto A, Esaki N, Inagaki K. Structure of the antitumour enzyme L-methionine gamma-lyase from Pseudomonas putida at 1.8 A resolution. J Biochem. 2007 Apr;141(4):535-44. Epub 2007 Feb 8. PMID:17289792 doi:http://dx.doi.org/10.1093/jb/mvm055
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