View source for 7tdl


==M379A mutant tyrosine phenol-lyase complexed with 3-bromo-DL-phenylalanine==
<StructureSection load='7tdl' size='340' side='right'caption='[[7tdl]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7tdl]] 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=7TDL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TDL 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]] 1.6&#8491;</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=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=OY3:(4Z)-4-({[(1E)-2-(3-bromophenyl)-1-carboxyethylidene]azaniumyl}methylidene)-2-methyl-5-[(phosphonooxy)methyl]-1,4-dihydropyridin-3-olate'>OY3</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=7tdl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tdl OCA], [https://pdbe.org/7tdl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tdl RCSB], [https://www.ebi.ac.uk/pdbsum/7tdl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tdl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TPL_CITFR TPL_CITFR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 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<ref>PMID:35577764</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7tdl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Citrobacter freundii]]
[[Category: Large Structures]]
[[Category: Phillips RS]]