Tryptophan synthase

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{{STRUCTURE_1wbj| PDB=1wbj | SIZE=400| SCENE=|right|CAPTION=Tryptophan synthase α subunit (grey) and β subunit (green) of the α2β2 tetramer complex with pyridoxal-phosphate, glycerol-3-phosphate and Na+ ion (purple) [[1wbj]]}}
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<StructureSection load='' size='350' side='right' caption='Tryptophan synthase α subunit (yellow, salmon) and β subunit (cyan, green) of the α2β2 tetramer complex with pyridoxal-phosphate, glycerol-3-phosphate and Na+ ion (purple) [[1wbj]]' scene='52/525189/Cv/5'>
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'''Tryptophan synthase''' (TrpS) is an α2β2 tetramer participating in the biosynthesis of tryptophan. TrpS α subunit catalyzes the formation of indole and glyceraldehyde-3-phosphate (G3P) from indole-3-glycerol phosphate (IGP). The β subunit catalyzes in a pyridoxal-phosphate (PLP) dependent reaction the formation of tryptophan (Trp) from indole and serine. The diffusion of indole from the α to the β subunit is facilitated via a hydrophobic channel connecting the subunits. TrpS is not found in animals hence it is tested as a possible drug target for tubertculosis, ocular and genital infections, cryptosporidiosis and as herbicide.
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== Function ==
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'''Tryptophan synthase''' (TrpS) is an α2β2 tetramer participating in the biosynthesis of tryptophan (Trp)<ref>PMID:11893063</ref>. TrpS '''α subunit''' catalyzes the formation of indole and glyceraldehyde-3-phosphate (G3P) from indole-3-glycerol phosphate (IGP). The '''β subunit''' catalyzes in a pyridoxal-phosphate (PLP) dependent reaction the formation of tryptophan (Trp) from indole and serine. The diffusion of indole from the α to the β subunit is facilitated via a hydrophobic channel connecting the subunits. '''Dimethylallyl tryptophan synthase''' (DMTS) catalyzes the alkylation of Trp by dimethylallyl phosphate to form 4-(γ,γ-dimethylallyl)-Trp<ref>PMID:1605639</ref>.
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===3D structures of tryptophan synthase===
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== Relevance ==
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TrpS is not found in animals hence it is tested as a possible drug target for tuberculosis, ocular and genital infections, cryptosporidiosis and as herbicide<ref>PMID:19430702</ref>.
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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== Structural highlights ==
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The <scene name='52/525189/Cv/6'>active site</scene> of TrpS subunit α contains the catalytic residues Glu and Asp<ref>PMID:16120446</ref>. Water molecules are shown as red spheres.
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==3D structures of tryptophan synthase==
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[[Tryptophan synthase 3D structures]]
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===TrpS α subunit===
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</StructureSection>
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[[3vnd]] - TrpS α subunit – ''Shewanella frigidimarina''<br />
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[[3tha]] - TrpS α subunit – ''Campylobacter jejuni''<br />
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[[3nav]] - TrpS α subunit – ''Vibrio cholerae''<br />
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[[1geq]] - PfTrpS α subunit - ''Pyrococcus furiosus''<br />
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[[2dzp]], [[2dzs]], [[2dzt]], [[2dzu]], [[2dzv]], [[2dzw]], [[2dzx]], [[2e09]] - PfTrpS α subunit (mutant)<br />
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[[1rd5]] - TrpS α subunit – corn<br />
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[[1ujp]] - TtTrpS α subunit <br />
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[[1v7y]], [[1wq5]], [[1xc4]] - EcTrpS α subunit <br />
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[[1xcf]] - EcTrpS α subunit (mutant)<br />
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[[2ekc]] - TrpS α subunit – ''Aquifex aeolicus''<br />
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''TrpS α binary complex''
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[[1wxj]] - TtTrpS α subunit + indole propanol phosphate<br />
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===TrpS β subunit===
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[[1x1q]] - TtTrpS β subunit – ''Thermus thermophilus''<br />
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[[2dh6]] - EcTrpS β subunit]] - ''Escherichia coli''<br />
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[[2o2e]], [[2o2j]] - TrpS β subunit – ''Mycobacterium tuberculosis''<br />
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[[1v8z]] - PfTrpS β subunit <br />
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[[4neg]] - TrpS β subunit – ''Bacillus anthracis''<br />
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''TrpS β binary complex''
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[[2dh5]] - EcTrpS β subunit + PLP<br />
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===TrpS α+β subunits===
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[[1wdw]] - PfTrpS α + β subunits <br />
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''TrpS α+β binary complex''
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[[1ttp]], [[1ttq]], [[1bks]], [[2wsy]], [[1kfk]] - StTrpS α + β + PLP – ''Salmonella typhimurium''<br />
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[[1a5a]], [[1k8x]] - StTrpS α (mutant) + β + PLP<br />
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[[1k7x]], [[2j9z]] - StTrpS α + β (mutant) + PLP<br />
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[[2tys]] - StTrpS α (mutant) + β (mutant) + Trp derivative<br />
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[[1kfe]] - StTrpS α (mutant) + β + pyridoxal-serine-monophsphate<br />
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[[1kfj]] - StTrpS α + β + pyridoxal-serine-monophsphate<br />
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[[2j9y]] - StTrpS α + β (mutant) + enoic acid derivative<br />
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[[3pr2]] - StTrpS α + β + inhibitor<br />
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[[4hn4]], [[4hpj]], [[4hpx]], [[4ht3]], [[4kkx]] - TrpS α + β + inhibitor – ''Salmonella enterica''<br />
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''TrpS α+β ternary complex with PLP and inhibitor''
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[[1a50]], [[1cw2]], [[1c9d]], [[1cx9]], [[1c8v]], [[1c29]], [[2cle]], [[2clh]], [[2cli]], [[2clk]], [[2cll]], [[2clm]], [[2clo]], [[2clf]] - StTrpS α + β + inhibitor + PLP<br />
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[[1fuy]] - StTrpS α + β (mutant) + inhibitor + PLP<br />
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''TrpS α+β ternary complex with PLP and IGP derivatives''
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[[1a5b]], [[1kfb]] - StTrpS α (mutant) + β + IGP + PLP<br />
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[[1k8z]] - StTrpS α + β (mutant) + IGP derivative + PLP<br />
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[[1kfc]] - StTrpS α (mutant) + β + IGP derivative + PLP<br />
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[[1k3u]], [[1k7e]], [[1k7f]] - StTrpS α + β + IGP derivative + PLP<br />
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[[1qoq]], [[2rh9]], [[2rhg]] - StTrpS α + β + IGP + PLP<br />
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[[1qop]] - StTrpS α + β + IGP analog + PLP<br />
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[[2trs]], [[1beu]] - StTrpS α (mutant) + β (mutant) + pyridoxal-serine-monophsphate + IGP analog
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''TrpS α+β ternary complex with PLP and G3P derivatives''
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[[1wbj]] - StTrpS α + β + G3P + PLP<br />
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[[2j9x]] - StTrpS α + β + G3P + acrylic acid derivative<br />
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[[1k8y]] - StTrpS α + β (mutant) + G3P derivative + PLP<br />
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[[1tjp]] - StTrpS α + β + G3P derivative + PLP<br />
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[[2tsy]] - StTrpS α (mutant) + β (mutant) + pyridoxal-serine-monophsphate + G3P
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[[1ubs]] - StTrpS α (mutant) + β (mutant) + serine + PLP<br />
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''TrpS α+β quaternary complex''
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[[1a5s]] - StTrpS α + β + serine + inhibitor + PLP<br />
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[[3cep]] - StTrpS α + β + G3P + indoline + PLP<br />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Tryptophan synthase α subunit (yellow, salmon) and β subunit (cyan, green) of the α2β2 tetramer complex with pyridoxal-phosphate, glycerol-3-phosphate and Na+ ion (purple) 1wbj

Drag the structure with the mouse to rotate

References

  1. ↑ Miles EW. Tryptophan synthase: a multienzyme complex with an intramolecular tunnel. Chem Rec. 2001;1(2):140-51. PMID:11893063
  2. ↑ Gebler JC, Poulter CD. Purification and characterization of dimethylallyl tryptophan synthase from Claviceps purpurea. Arch Biochem Biophys. 1992 Jul;296(1):308-13. PMID:1605639 doi:10.1016/0003-9861(92)90577-j
  3. ↑ Shen H, Yang Y, Wang F, Zhang Y, Ye N, Xu S, Wang H. Characterization of the putative tryptophan synthase beta-subunit from Mycobacterium tuberculosis. Acta Biochim Biophys Sin (Shanghai). 2009 May;41(5):379-88. PMID:19430702
  4. ↑ Kulik V, Hartmann E, Weyand M, Frey M, Gierl A, Niks D, Dunn MF, Schlichting I. On the structural basis of the catalytic mechanism and the regulation of the alpha subunit of tryptophan synthase from Salmonella typhimurium and BX1 from maize, two evolutionarily related enzymes. J Mol Biol. 2005 Sep 23;352(3):608-20. PMID:16120446 doi:10.1016/j.jmb.2005.07.014

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Michal Harel, Alexander Berchansky, Joel L. Sussman, Amer Ali

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