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| | <StructureSection load='6hte' size='340' side='right'caption='[[6hte]], [[Resolution|resolution]] 1.96Å' scene=''> | | <StructureSection load='6hte' size='340' side='right'caption='[[6hte]], [[Resolution|resolution]] 1.96Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6hte]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HTE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HTE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6hte]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6eqn 6eqn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HTE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 1.961Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trpB2, SSO1145 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=6hte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hte OCA], [https://pdbe.org/6hte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hte RCSB], [https://www.ebi.ac.uk/pdbsum/6hte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hte 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=6hte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hte OCA], [http://pdbe.org/6hte PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hte RCSB], [http://www.ebi.ac.uk/pdbsum/6hte PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hte ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TRPB2_SULSO TRPB2_SULSO]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | + | [https://www.uniprot.org/uniprot/TRPB2_SACS2 TRPB2_SACS2] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. |
| | <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 6hte" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6hte" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 35091]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Tryptophan synthase]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Bucher, R]] | + | [[Category: Bucher R]] |
| - | [[Category: Fleming, J]] | + | [[Category: Fleming J]] |
| - | [[Category: Mayans, O]] | + | [[Category: Mayans O]] |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
TRPB2_SACS2 The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Publication Abstract from PubMed
Tryptophan synthase (TrpS) is a heterotetrameric alphabetabetaalpha enzyme that exhibits complex substrate channeling and allosteric mechanisms and is a model system in enzymology. In this work, we characterize proposed early and late evolutionary states of TrpS and show that they have distinct quaternary structures, caused by insertions-deletions of sequence segments (indels) in the beta-subunit. Remarkably, indole hydrophobic channels that connect alpha and beta active sites have re-emerged in both TrpS types, yet they follow different paths through the beta-subunit fold. Also, both TrpS geometries activate the alpha-subunit through the rearrangement of loops flanking the active site. Our results link evolutionary sequence changes in the enzyme subunits with channeling and allostery in the TrpS enzymes. The findings demonstrate that indels allow protein quaternary architectures to scape "minima" in the evolutionary landscape, thereby overcoming the conservational constraints imposed by existing functional interfaces and being free to morph into new mechanistic enzymes.
Evolutionary Morphing of Tryptophan Synthase: Functional Mechanisms for the Enzymatic Channeling of Indole.,Fleming JR, Schupfner M, Busch F, Basle A, Ehrmann A, Sterner R, Mayans O J Mol Biol. 2018 Oct 24. pii: S0022-2836(18)30606-5. doi:, 10.1016/j.jmb.2018.10.013. PMID:30367843[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fleming JR, Schupfner M, Busch F, Basle A, Ehrmann A, Sterner R, Mayans O. Evolutionary Morphing of Tryptophan Synthase: Functional Mechanisms for the Enzymatic Channeling of Indole. J Mol Biol. 2018 Oct 24. pii: S0022-2836(18)30606-5. doi:, 10.1016/j.jmb.2018.10.013. PMID:30367843 doi:http://dx.doi.org/10.1016/j.jmb.2018.10.013
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