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| | ==Citrobacter freundii tyrosine phenol-lyase F448A mutant== | | ==Citrobacter freundii tyrosine phenol-lyase F448A mutant== |
| - | <StructureSection load='6dxv' size='340' side='right' caption='[[6dxv]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='6dxv' size='340' side='right'caption='[[6dxv]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6dxv]] 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=6DXV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DXV FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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='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='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='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> |
| - | <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=6dxv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dxv OCA], [http://pdbe.org/6dxv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dxv RCSB], [http://www.ebi.ac.uk/pdbsum/6dxv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dxv 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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| | </div> | | </div> |
| | <div class="pdbe-citations 6dxv" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6dxv" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Tyrosinase 3D structures|Tyrosinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium freundii braak 1928]] | + | [[Category: Citrobacter freundii]] |
| - | [[Category: Tyrosine phenol-lyase]] | + | [[Category: Large Structures]] |
| - | [[Category: Phillips, R S]] | + | [[Category: Phillips RS]] |
| - | [[Category: Aminotransferase fold]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Pyridoxal-5'-phosphate]]
| + | |
| Structural highlights
Function
TPL_CITFR
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., & 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Phillips RS, Craig S. Crystal Structures of Wild-type and F448A Mutant Citrobacter freundii Tyrosine Phenol-lyase Complexed with Substrate and Inhibitors: Implications for the Reaction Mechanism. Biochemistry. 2018 Sep 27. doi: 10.1021/acs.biochem.8b00724. PMID:30260636 doi:http://dx.doi.org/10.1021/acs.biochem.8b00724
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