Tryptophan synthase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{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]]}}
 
-
'''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.
+
<StructureSection load='1wbj' size='340' side='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]]' scene=''>
 +
== Function ==
 +
'''Tryptophan synthase''' (TrpS) is an α2β2 tetramer participating in the biosynthesis of tryptophan<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.
 +
== Relevance ==
 +
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>.
 +
 +
== Structural highlights ==
 +
The active site of TrpS subunit α contains the catalytic residues Glu and Asp which interact with G3P<ref>PMID:16120446</ref>.
 +
 +
</StructureSection>
==3D structures of tryptophan synthase==
==3D structures of tryptophan synthase==
Line 84: Line 92:
**[[3cep]] - StTrpS α + β + G3P + indoline + PLP<br />
**[[3cep]] - StTrpS α + β + G3P + indoline + PLP<br />
}}
}}
 +
== References ==
 +
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 08:54, 27 September 2016

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

Drag the structure with the mouse to rotate

3D structures of tryptophan synthase

Updated on 27-September-2016

References

  1. ↑ Miles EW. Tryptophan synthase: a multienzyme complex with an intramolecular tunnel. Chem Rec. 2001;1(2):140-51. PMID:11893063
  2. ↑ 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
  3. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

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

Retrieved from "http://52.214.119.220/wiki/index.php/Tryptophan_synthase"
Personal tools