7tcs: Difference between revisions
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<StructureSection load='7tcs' size='340' side='right'caption='[[7tcs]], [[Resolution|resolution]] 1.37Å' scene=''> | <StructureSection load='7tcs' size='340' side='right'caption='[[7tcs]], [[Resolution|resolution]] 1.37Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7tcs]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TCS FirstGlance]. <br> | <table><tr><td colspan='2'>[[7tcs]] is a 4 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=7TCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TCS FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PN9:(4Z)-4-({[(1E)-1-carboxy-3-(methylsulfanyl)propylidene]azaniumyl}methylidene)-2-methyl-5-[(phosphonooxy)methyl]-1,4-dihydropyridin-3-olate'>PN9</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PN9:(4Z)-4-({[(1E)-1-carboxy-3-(methylsulfanyl)propylidene]azaniumyl}methylidene)-2-methyl-5-[(phosphonooxy)methyl]-1,4-dihydropyridin-3-olate'>PN9</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=7tcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tcs OCA], [https://pdbe.org/7tcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tcs RCSB], [https://www.ebi.ac.uk/pdbsum/7tcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tcs ProSAT]</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=7tcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tcs OCA], [https://pdbe.org/7tcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tcs RCSB], [https://www.ebi.ac.uk/pdbsum/7tcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tcs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/TPL_CITFR TPL_CITFR]] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Citrobacter freundii]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Phillips RS]] | |||
[[Category: Phillips | |||
Revision as of 08:28, 8 September 2022
M379A mutant tyrosine phenol-lyase complexed with L-methionineM379A mutant tyrosine phenol-lyase complexed with L-methionine
Structural highlights
FunctionPublication Abstract from PubMedThe M379A mutant of Citrobacter freundii tyrosine phenol-lyase (TPL) has been prepared. M379A TPL is a robust catalyst to prepare a number of tyrosines substituted at the 3-position with bulky groups that cannot be made with wild type TPL. The three dimensional structures of M379A TPL complexed with L-methionine and 3-bromo-DL-phenylalanine have been determined by X-ray crystallography. Methionine is bound as a quinonoid complex in a closed active site in 3 of 4 chains of homotetrameric M379A TPL. M379A TPL reacts with L-methionine about 8-fold slower than wild type TPL. The temperature dependence shows that the slower reaction is due to less positive activation entropy. The structure of the M379A TPL complex of 3-bromo-DL-phenylalanine has a quinonoid complex in two subunits, with an open active site conformation. The effects of the M379A mutation on TPL suggest that the mutant enzyme has altered the conformational dynamics of the active site. M379A Mutant Tyrosine Phenol-lyase from Citrobacter freundii Has Altered Conformational Dynamics.,Phillips RS, Jones B, Nash S Chembiochem. 2022 Jul 5;23(13):e202200028. doi: 10.1002/cbic.202200028. Epub 2022, May 24. PMID:35577764[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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