View source for 6dvx


==Citrobacter freundii tyrosine phenol-lyase F448A mutant complexed with L-phenylalanine==
<StructureSection load='6dvx' size='340' side='right' caption='[[6dvx]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6dvx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_freundii"_braak_1928 "bacterium freundii" braak 1928]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DVX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DVX FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene>, <scene name='pdbligand=P70:(E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-phenylalanine'>P70</scene>, <scene name='pdbligand=P71:(2E)-2-{[(Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1H)-ylidene}methyl]imino}-3-phenylpropanoic+acid'>P71</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6dur|6dur]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tpl ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=546 "Bacterium freundii" Braak 1928])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tyrosine_phenol-lyase Tyrosine phenol-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.2 4.1.99.2] </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=6dvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dvx OCA], [http://pdbe.org/6dvx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dvx RCSB], [http://www.ebi.ac.uk/pdbsum/6dvx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dvx ProSAT]</span></td></tr>
</table>
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== 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>
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<div class="pdbe-citations 6dvx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacterium freundii braak 1928]]
[[Category: Tyrosine phenol-lyase]]
[[Category: Phillips, R S]]
[[Category: Aminotransferase fold]]
[[Category: Lyase]]
[[Category: Pyridoxal-5'-phosphate]]