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| | ==Crystal structure of Tryptophan synthase alpha chain homolog BX1: a member of the chemical plant defense system== | | ==Crystal structure of Tryptophan synthase alpha chain homolog BX1: a member of the chemical plant defense system== |
| - | <StructureSection load='1rd5' size='340' side='right' caption='[[1rd5]], [[Resolution|resolution]] 2.02Å' scene=''> | + | <StructureSection load='1rd5' size='340' side='right'caption='[[1rd5]], [[Resolution|resolution]] 2.02Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rd5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Maize Maize]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RD5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1RD5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rd5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RD5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLA:MALONIC+ACID'>MLA</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]] 2.02Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bks|1bks]], [[1kfk|1kfk]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] </span></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=1rd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rd5 OCA], [https://pdbe.org/1rd5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rd5 RCSB], [https://www.ebi.ac.uk/pdbsum/1rd5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rd5 ProSAT]</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=1rd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rd5 OCA], [http://pdbe.org/1rd5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rd5 RCSB], [http://www.ebi.ac.uk/pdbsum/1rd5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rd5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TRPA_MAIZE TRPA_MAIZE]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In bacteria, tryptophan synthase alpha (TSA) activity is almost completely dependent on formation of an active alpha2beta2 complex with tryptophan synthase beta (TSB), and indole is usually not released during tryptophan synthesis. In maize, the TSA homolog BX1 catalyzes the formation of free indole from indole-3-glycerol phosphate, independently of TSB.<ref>PMID:9235894</ref> | + | [https://www.uniprot.org/uniprot/TRPA_MAIZE TRPA_MAIZE] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In bacteria, tryptophan synthase alpha (TSA) activity is almost completely dependent on formation of an active alpha2beta2 complex with tryptophan synthase beta (TSB), and indole is usually not released during tryptophan synthesis. In maize, the TSA homolog BX1 catalyzes the formation of free indole from indole-3-glycerol phosphate, independently of TSB.<ref>PMID:9235894</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rd/1rd5_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rd/1rd5_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1rd5" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1rd5" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Maize]] | + | [[Category: Large Structures]] |
| - | [[Category: Tryptophan synthase]] | + | [[Category: Zea mays]] |
| - | [[Category: Dunn, M F]] | + | [[Category: Dunn MF]] |
| - | [[Category: Frey, M]] | + | [[Category: Frey M]] |
| - | [[Category: Gierl, A]] | + | [[Category: Gierl A]] |
| - | [[Category: Hartmann, E]] | + | [[Category: Hartmann E]] |
| - | [[Category: Kulik, V]] | + | [[Category: Kulik V]] |
| - | [[Category: Niks, D]] | + | [[Category: Niks D]] |
| - | [[Category: Schlichting, I]] | + | [[Category: Schlichting I]] |
| - | [[Category: Weyand, M]] | + | [[Category: Weyand M]] |
| - | [[Category: Diboa]]
| + | |
| - | [[Category: Dimboa]]
| + | |
| - | [[Category: Hydroxamic acid]]
| + | |
| - | [[Category: Indole]]
| + | |
| - | [[Category: Indole-glycerol-phosphate]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
TRPA_MAIZE The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In bacteria, tryptophan synthase alpha (TSA) activity is almost completely dependent on formation of an active alpha2beta2 complex with tryptophan synthase beta (TSB), and indole is usually not released during tryptophan synthesis. In maize, the TSA homolog BX1 catalyzes the formation of free indole from indole-3-glycerol phosphate, independently of TSB.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Indole is a reaction intermediate in at least two biosynthetic pathways in maize seedlings. In the primary metabolism, the alpha-subunit (TSA) of the bifunctional tryptophan synthase (TRPS) catalyzes the cleavage of indole 3-glycerol phosphate (IGP) to indole and d-glyceraldehyde 3-phosphate (G3P). Subsequently, indole diffuses through the connecting tunnel to the beta-active site where it is condensed with serine to form tryptophan and water. The maize enzyme, BX1, a homolog of TSA, also cleaves IGP to G3P and indole, and the indole is further converted to 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one, a secondary plant metabolite. BX1 cleaves IGP significantly faster to G3P and indole than does TSA. In line with their different biological functions, these two evolutionary related enzymes differ significantly in their regulatory aspects while catalyzing the same chemistry. Here, the mechanism of IGP cleavage by TSA was analyzed using a novel transition state analogue generated in situ by reaction of 2-aminophenol and G3P. The crystal structure of the complex shows an sp3-hybridized atom corresponding to the C3 position of IGP. The catalytic alphaGlu49 rotates to interact with the sp3-hybridized atom and the 3' hydroxyl group suggesting that it serves both as proton donor and acceptor in the alpha-reaction. The second catalytic residue, alphaAsp60 interacts with the atom corresponding to the indolyl nitrogen, and the catalytically important loop alphaL6 is in the closed, high activity conformation. Comparison of the TSA and TSA-transition state analogue structures with the crystal structure of BX1 suggests that the faster catalytic rate of BX1 may be due to a stabilization of the active conformation: loop alphaL6 is closed and the catalytic glutamate is in the active conformation. The latter is caused by a substitution of the residues that stabilize the inactive conformation in TRPS.
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.,Kulik V, Hartmann E, Weyand M, Frey M, Gierl A, Niks D, Dunn MF, Schlichting I J Mol Biol. 2005 Sep 23;352(3):608-20. PMID:16120446[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Frey M, Chomet P, Glawischnig E, Stettner C, Grun S, Winklmair A, Eisenreich W, Bacher A, Meeley RB, Briggs SP, Simcox K, Gierl A. Analysis of a chemical plant defense mechanism in grasses. Science. 1997 Aug 1;277(5326):696-9. PMID:9235894
- ↑ 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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