4oma
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The crystal structure of methionine gamma-lyase from Citrobacter freundii in complex with L-cycloserine pyridoxal-5'-phosphate== |
| + | <StructureSection load='4oma' size='340' side='right'caption='[[4oma]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4oma]] 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=4OMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OMA 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]] 1.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LCS:[5-HYDROXY-6-METHYL-4-({[(4E)-3-OXO-1,2-OXAZOLIDIN-4-YLIDENE]AMINO}METHYL)PYRIDIN-3-YL]METHYL+DIHYDROGEN+PHOSPHATE'>LCS</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=4oma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oma OCA], [https://pdbe.org/4oma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oma RCSB], [https://www.ebi.ac.uk/pdbsum/4oma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oma ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q84AR1_CITFR Q84AR1_CITFR] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | MGL catalyzes the gamma-elimination of L-methionine and its derivatives as well as the beta-elimination of L-cysteine and its analogs. These reactions yield alpha-keto acids and thiols. The mechanism of chemical conversion of amino acids includes numerous reaction intermediates. The detailed analysis of MGL interaction with glycine, L-alanine, L-norvaline and L-cycloserine was performed by pre-steady-state stopped-flow kinetics. The structure of side chains of the amino acids is important both for their binding with enzyme and for the stability of the external aldimine and ketimine intermediates. X-ray structure of MGL-L-cycloserine complex has been solved at 1.6 A resolution. The structure models ketimine intermediate of physiological reaction. The results elucidate the mechanisms of the intermediates interconversion at the stages of external aldimine and ketimine formation. | ||
| - | + | Pre-Steady-State Kinetic and Structural Analysis of Interaction of Methionine gamma-Lyase from Citrobacter freundii with Inhibitors.,Kuznetsov NA, Faleev NG, Kuznetsova AA, Morozova EA, Revtovich SV, Anufrieva NV, Nikulin AD, Fedorova OS, Demidkina TV J Biol Chem. 2014 Nov 14. pii: jbc.M114.586511. PMID:25398880<ref>PMID:25398880</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4oma" 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]] | ||
Current revision
The crystal structure of methionine gamma-lyase from Citrobacter freundii in complex with L-cycloserine pyridoxal-5'-phosphate
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