3jw9
From Proteopedia
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- | + | ==Crystal structure of L-methionine gamma-lyase from Citrobacter freundii with S-ethyl-cysteine== | |
- | + | <StructureSection load='3jw9' size='340' side='right' caption='[[3jw9]], [[Resolution|resolution]] 1.80Å' scene=''> | |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3jw9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JW9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JW9 FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ECX:S-ETHYL-L-CYSTEINE'>ECX</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | ||
+ | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2rfv|2rfv]], [[1y4i|1y4i]], [[2o7c|2o7c]], [[1ukj|1ukj]], [[1e5e|1e5e]], [[3jwa|3jwa]], [[3jwb|3jwb]]</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=3jw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jw9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3jw9 RCSB], [http://www.ebi.ac.uk/pdbsum/3jw9 PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jw/3jw9_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Crystal structures of Citrobacter freundii methionine gamma-lyase complexes with the substrates of gamma- (L-1-amino-3-methylthiopropylphosphinic acid) and beta- (S-ethyl-L-cysteine) elimination reactions and the competitive inhibitor L-norleucine have been determined at 1.45, 1.8, and 1.63 A resolution, respectively. All three amino acids occupy the active site of the enzyme but do not form a covalent bond with pyridoxal 5'-phosphate. Hydrophobic interactions between the active site residues and the side groups of the substrates and the inhibitor are supposed to cause noncovalent binding. Arg374 and Ser339 are involved in the binding of carboxyl groups of the substrates and the inhibitor. The hydroxyl of Tyr113 is a potential acceptor of a proton from the amino groups of the amino acids. | ||
- | + | Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine gamma-lyase with substrates.,Revtovich SV, Morozova EA, Khurs EN, Zakomirdina LN, Nikulin AD, Demidkina TV, Khomutov RM Biochemistry (Mosc). 2011 May;76(5):564-70. doi: 10.1134/S0006297911050063. PMID:21639836<ref>PMID:21639836</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Methionine gamma-lyase]] | [[Category: Methionine gamma-lyase]] | ||
[[Category: Demidkina, T V.]] | [[Category: Demidkina, T V.]] |
Revision as of 06:39, 5 November 2014
Crystal structure of L-methionine gamma-lyase from Citrobacter freundii with S-ethyl-cysteine
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