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2cll

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{{Seed}}
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==TRYPTOPHAN SYNTHASE (EXTERNAL ALDIMINE STATE) IN COMPLEX WITH N-(4'-TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-ETHYLPHOSPHATE (F9)==
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[[Image:2cll.png|left|200px]]
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<StructureSection load='2cll' size='340' side='right' caption='[[2cll]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2cll]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CLL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CLL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F9F:2-({[4-(TRIFLUOROMETHOXY)PHENYL]SULFONYL}AMINO)ETHYL+DIHYDROGEN+PHOSPHATE'>F9F</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLS:[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-SERINE'>PLS</scene></td></tr>
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<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]], [[1ttq|1ttq]], [[1ubs|1ubs]], [[1wbj|1wbj]], [[2cle|2cle]], [[2clf|2clf]], [[2cli|2cli]], [[2clk|2clk]], [[2clm|2clm]], [[2clo|2clo]], [[2trs|2trs]], [[2tsy|2tsy]], [[2tys|2tys]], [[2wsy|2wsy]]</td></tr>
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<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>
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<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=2cll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cll OCA], [http://pdbe.org/2cll PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cll RCSB], [http://www.ebi.ac.uk/pdbsum/2cll PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cl/2cll_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2cll ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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 &gt;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].
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<!--
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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<ref>PMID:17559232</ref>
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The line below this paragraph, containing "STRUCTURE_2cll", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_2cll| PDB=2cll | SCENE= }}
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===TRYPTOPHAN SYNTHASE (EXTERNAL ALDIMINE STATE) IN COMPLEX WITH N-(4'-TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-ETHYLPHOSPHATE (F9)===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2cll" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Tryptophan synthase|Tryptophan synthase]]
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The line below this paragraph, {{ABSTRACT_PUBMED_17559232}}, adds the Publication Abstract to the page
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== References ==
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(as it appears on PubMed at http://www.pubmed.gov), where 17559232 is the PubMed ID number.
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<references/>
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__TOC__
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{{ABSTRACT_PUBMED_17559232}}
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</StructureSection>
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==About this Structure==
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2CLL is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CLL OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17559232 17559232]
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[[Category: Protein complex]]
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[[Category: Salmonella typhimurium]]
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[[Category: Tryptophan synthase]]
[[Category: Tryptophan synthase]]
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[[Category: Barends, T R.]]
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[[Category: Barends, T R]]
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[[Category: Blumenstein, L.]]
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[[Category: Blumenstein, L]]
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[[Category: Dunn, M F.]]
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[[Category: Dunn, M F]]
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[[Category: Harris, R.]]
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[[Category: Harris, R]]
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[[Category: Kimmich, N.]]
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[[Category: Kimmich, N]]
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[[Category: Kulik, V.]]
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[[Category: Kulik, V]]
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[[Category: Ngo, H.]]
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[[Category: Ngo, H]]
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[[Category: Niks, D.]]
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[[Category: Niks, D]]
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[[Category: Schlichting, I.]]
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[[Category: Schlichting, I]]
[[Category: Allosteric enzyme]]
[[Category: Allosteric enzyme]]
[[Category: Amino-acid biosynthesis]]
[[Category: Amino-acid biosynthesis]]
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[[Category: Pyridoxal phosphate]]
[[Category: Pyridoxal phosphate]]
[[Category: Tryptophan biosynthesis]]
[[Category: Tryptophan biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:40:58 2008''
 

Current revision

TRYPTOPHAN SYNTHASE (EXTERNAL ALDIMINE STATE) IN COMPLEX WITH N-(4'-TRIFLUOROMETHOXYBENZENESULFONYL)-2-AMINO-1-ETHYLPHOSPHATE (F9)

2cll, resolution 1.60Å

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