View source for 6dxv


==Citrobacter freundii tyrosine phenol-lyase F448A mutant==
<StructureSection load='6dxv' size='340' side='right'caption='[[6dxv]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6dxv]] is a 2 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=6DXV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DXV 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6dxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dxv OCA], [https://pdbe.org/6dxv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dxv RCSB], [https://www.ebi.ac.uk/pdbsum/6dxv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dxv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TPL_CITFR TPL_CITFR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Tyrosine phenol-lyase (TPL; E.C. 4.1.99.2) is a pyridoxal-5'-phosphate dependent enzyme that catalyzes the reversible hydrolytic cleavage of L-tyrosine to phenol and ammonium pyruvate. We have shown previously that F448A TPL has kcat and kcat/Km values for L-tyrosine reduced by about 104 (Phillips, R. S., Vita, A., Spivey, J. B., Rudloff, A. P., Driscoll, M. D., &amp; Hay, S. (2016) ACS Catalysis, 6, 6770-6779). We have now obtained crystal structures of F448A TPL and complexes with L-alanine, L-methionine, L-phenylalanine, and 3-F-L-tyrosine at 2.05-2.27 A, as well as the complex of wild-type TPL with L-phenylalanine at 1.8 A. The small domain of F448A TPL, where Phe-448 is located, is more disordered in chain A than wild-type TPL. The complexes of F448A TPL with L-alanine and L-phenylalanine are in an open conformation in both chains, while the complex with L-methionine is a 52:48 equilibrium mixture of open and closed conformations, respectively, in chain A. Wild-type TPL with L-alanine is closed in chain A and open in chain B, and the complex with L-phenylalanine is 56:44 in open and closed conformations in chain A. Thus, the Phe-448 to alanine mutation affects the conformational equilibrium of open and closed active sites. The structure of the 3-F-L-tyrosine quinonoid complex of F448A TPL is unstrained and in an open conformation, with a hydrogen bond from the phenolic OH to Thr-124. These results support our previous conclusion that ground-state strain plays a critical role in the mechanism of TPL.

Crystal Structures of Wild-type and F448A Mutant Citrobacter freundii Tyrosine Phenol-lyase Complexed with Substrate and Inhibitors: Implications for the Reaction Mechanism.,Phillips RS, Craig S Biochemistry. 2018 Sep 27. doi: 10.1021/acs.biochem.8b00724. PMID:30260636<ref>PMID:30260636</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6dxv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tyrosinase 3D structures|Tyrosinase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Citrobacter freundii]]
[[Category: Large Structures]]
[[Category: Phillips RS]]