2j9x

From Proteopedia

(Difference between revisions)

Revision as of 08:04, 19 January 2022

Tryptophan Synthase in complex with GP, alpha-D,L-glycerol-phosphate, Cs, pH6.5 - alpha aminoacrylate form - (GP)E(A-A)

Structural highlights

2j9x is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	1a50, 1a5a, 1a5b, 1a5s, 1beu, 1bks, 1c29, 1c8v, 1c9d, 1cw2, 1cx9, 1fuy, 1k3u, 1k7e, 1k7f, 1k7x, 1k8x, 1k8y, 1k8z, 1kfb, 1kfc, 1kfe, 1kfj, 1kfk, 1qop, 1qoq, 1tjp, 1ttp, 1ubs, 1wbj, 2cle, 2clf, 2cli, 2clk, 2cll, 2clm, 2clo, 2trs, 2tsy, 2tys, 2wsy, 2j9y, 2j9z
Activity:	Tryptophan synthase, with EC number 4.2.1.20
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TRPA_SALTY] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [TRPB_SALTY] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.

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

In the tryptophan synthase bienzyme complex, indole produced by substrate cleavage at the alpha-site is channeled to the beta-site via a 25 A long tunnel. Within the beta-site, indole and l-Ser react with pyridoxal 5'-phosphate in a two-stage reaction to give l-Trp. In stage I, l-Ser forms an external aldimine, E(Aex1), which converts to the alpha-aminoacrylate aldimine, E(A-A). Formation of E(A-A) at the beta-site activates the alpha-site >30-fold. In stage II, indole reacts with E(A-A) to give l-Trp. The binding of alpha-site ligands (ASLs) exerts strong allosteric effects on the reaction of substrates at the beta-site: the distribution of intermediates formed in stage I is shifted in favor of E(A-A), and the binding of ASLs triggers a conformational change in the beta-site to a state with an increased affinity for l-Ser. Here, we compare the behavior of new ASLs as allosteric effectors of stage I with the behavior of the natural product, d-glyceraldehyde 3-phosphate. Rapid kinetics and kinetic isotope effects show these ASLs bind with affinities ranging from micro- to millimolar, and the rate-determining step for conversion of E(Aex1) to E(A-A) is increased by 8-10-fold. To derive a structure-based mechanism for stage I, X-ray structures of both the E(Aex1) and E(A-A) states complexed with the different ASLs were determined and compared with structures of the ASL complexes with the internal aldimine [Ngo, H., Harris, R., Kimmich, N., Casino, P., Niks, D., Blumenstein, L., Barends, T. R., Kulik, V., Weyand, M., Schlichting, I., and Dunn, M. F. (2007) Biochemistry 46, 7713-7727].

Allosteric regulation of substrate channeling in tryptophan synthase: modulation of the L-serine reaction in stage I of the beta-reaction by alpha-site ligands.,Ngo H, Kimmich N, Harris R, Niks D, Blumenstein L, Kulik V, Barends TR, Schlichting I, Dunn MF Biochemistry. 2007 Jul 3;46(26):7740-53. Epub 2007 Jun 9. PMID:17559232^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ngo H, Kimmich N, Harris R, Niks D, Blumenstein L, Kulik V, Barends TR, Schlichting I, Dunn MF. Allosteric regulation of substrate channeling in tryptophan synthase: modulation of the L-serine reaction in stage I of the beta-reaction by alpha-site ligands. Biochemistry. 2007 Jul 3;46(26):7740-53. Epub 2007 Jun 9. PMID:17559232 doi:10.1021/bi7003872

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2j9x"

@@ Line 3: / Line 3: @@
 <StructureSection load='2j9x' size='340' side='right'caption='[[2j9x]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2j9x]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J9X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2J9X FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2j9x]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J9X FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CS:CESIUM+ION'>CS</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=G3P:SN-GLYCEROL-3-PHOSPHATE'>G3P</scene>, <scene name='pdbligand=P1T:2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]ACRYLIC+ACID'>P1T</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a50|1a50]], [[1a5a|1a5a]], [[1a5b|1a5b]], [[1a5s|1a5s]], [[1beu|1beu]], [[1bks|1bks]], [[1c29|1c29]], [[1c8v|1c8v]], [[1c9d|1c9d]], [[1cw2|1cw2]], [[1cx9|1cx9]], [[1fuy|1fuy]], [[1k3u|1k3u]], [[1k7e|1k7e]], [[1k7f|1k7f]], [[1k7x|1k7x]], [[1k8x|1k8x]], [[1k8y|1k8y]], [[1k8z|1k8z]], [[1kfb|1kfb]], [[1kfc|1kfc]], [[1kfe|1kfe]], [[1kfj|1kfj]], [[1kfk|1kfk]], [[1qop|1qop]], [[1qoq|1qoq]], [[1tjp|1tjp]], [[1ttp|1ttp]], [[1ubs|1ubs]], [[1wbj|1wbj]], [[2cle|2cle]], [[2clf|2clf]], [[2cli|2cli]], [[2clk|2clk]], [[2cll|2cll]], [[2clm|2clm]], [[2clo|2clo]], [[2trs|2trs]], [[2tsy|2tsy]], [[2tys|2tys]], [[2wsy|2wsy]], [[2j9y|2j9y]], [[2j9z|2j9z]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a50|1a50]], [[1a5a|1a5a]], [[1a5b|1a5b]], [[1a5s|1a5s]], [[1beu|1beu]], [[1bks|1bks]], [[1c29|1c29]], [[1c8v|1c8v]], [[1c9d|1c9d]], [[1cw2|1cw2]], [[1cx9|1cx9]], [[1fuy|1fuy]], [[1k3u|1k3u]], [[1k7e|1k7e]], [[1k7f|1k7f]], [[1k7x|1k7x]], [[1k8x|1k8x]], [[1k8y|1k8y]], [[1k8z|1k8z]], [[1kfb|1kfb]], [[1kfc|1kfc]], [[1kfe|1kfe]], [[1kfj|1kfj]], [[1kfk|1kfk]], [[1qop|1qop]], [[1qoq|1qoq]], [[1tjp|1tjp]], [[1ttp|1ttp]], [[1ubs|1ubs]], [[1wbj|1wbj]], [[2cle|2cle]], [[2clf|2clf]], [[2cli|2cli]], [[2clk|2clk]], [[2cll|2cll]], [[2clm|2clm]], [[2clo|2clo]], [[2trs|2trs]], [[2tsy|2tsy]], [[2tys|2tys]], [[2wsy|2wsy]], [[2j9y|2j9y]], [[2j9z|2j9z]]</div></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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [https://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'>[http://proteopedia.org/fgij/fg.htm?mol=2j9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j9x OCA], [http://pdbe.org/2j9x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j9x RCSB], [http://www.ebi.ac.uk/pdbsum/2j9x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j9x ProSAT]</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=2j9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j9x OCA], [https://pdbe.org/2j9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j9x RCSB], [https://www.ebi.ac.uk/pdbsum/2j9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j9x ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/TRPA_SALTY TRPA_SALTY]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [[http://www.uniprot.org/uniprot/TRPB_SALTY TRPB_SALTY]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
+[[https://www.uniprot.org/uniprot/TRPA_SALTY TRPA_SALTY]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [[https://www.uniprot.org/uniprot/TRPB_SALTY TRPB_SALTY]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2j9x

From Proteopedia

Revision as of 08:04, 19 January 2022

Tryptophan Synthase in complex with GP, alpha-D,L-glycerol-phosphate, Cs, pH6.5 - alpha aminoacrylate form - (GP)E(A-A)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox