1kfb

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[[Image:1kfb.jpg|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF TRYPTOPHAN SYNTHASE FROM SALMONELLA TYPHIMURIUM WITH Indole Glycerol Phosphate==
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|PDB= 1kfb |SIZE=350|CAPTION= <scene name='initialview01'>1kfb</scene>, resolution 1.90&Aring;
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<StructureSection load='1kfb' size='340' side='right'caption='[[1kfb]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=IGP:INDOLE-3-GLYCEROL+PHOSPHATE'>IGP</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
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<table><tr><td colspan='2'>[[1kfb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFB FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IGP:INDOLE-3-GLYCEROL+PHOSPHATE'>IGP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfb OCA], [https://pdbe.org/1kfb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfb RCSB], [https://www.ebi.ac.uk/pdbsum/1kfb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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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/kf/1kfb_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=1kfb ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF TRYPTOPHAN SYNTHASE FROM SALMONELLA TYPHIMURIUM WITH Indole Glycerol Phosphate'''
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==See Also==
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*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The catalytic activity and substrate channeling of the pyridoxal 5'-phosphate-dependent tryptophan synthase alpha(2)beta(2) complex is regulated by allosteric interactions that modulate the switching of the enzyme between open, low activity and closed, high activity states during the catalytic cycle. The highly conserved alphaThr183 residue is part of loop alphaL6 and is located next to the alpha-active site and forms part of the alpha-beta subunit interface. The role of the interactions of alphaThr183 in alpha-site catalysis and allosteric regulation was investigated by analyzing the kinetics and crystal structures of the isosteric mutant alphaThr183Val. The mutant displays strongly impaired allosteric alpha-beta communication, and the catalytic activity of the alpha-reaction is reduced one hundred fold, whereas the beta-activity is not affected. The structural work establishes that the basis for the missing inter-subunit signaling is the lack of loop alphaL6 closure even in the presence of the alpha-subunit ligands, 3-indolyl-D-glycerol 3'-phosphate, or 3-indolylpropanol 3'-phosphate. The structural basis for the reduced alpha-activity has its origins in the missing hydrogen bond between alphaThr183 and the catalytic residue, alphaAsp60.
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[[Category: Large Structures]]
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[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
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==About this Structure==
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[[Category: Arac D]]
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1KFB 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=1KFB OCA].
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[[Category: Dunn MF]]
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[[Category: Kulik V]]
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==Reference==
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[[Category: Niks D]]
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On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase., Kulik V, Weyand M, Seidel R, Niks D, Arac D, Dunn MF, Schlichting I, J Mol Biol. 2002 Dec 6;324(4):677-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12460570 12460570]
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[[Category: Schlichting I]]
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[[Category: Protein complex]]
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[[Category: Siedel R]]
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[[Category: Salmonella typhimurium]]
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[[Category: Weyand M]]
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[[Category: Arac, D.]]
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[[Category: Dunn, M F.]]
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[[Category: Kulik, V.]]
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[[Category: Niks, D.]]
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[[Category: Schlichting, I.]]
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[[Category: Siedel, R.]]
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[[Category: Weyand, M.]]
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[[Category: IGP]]
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[[Category: PLP]]
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[[Category: helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:28:48 2008''
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Current revision

CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF TRYPTOPHAN SYNTHASE FROM SALMONELLA TYPHIMURIUM WITH Indole Glycerol Phosphate

PDB ID 1kfb

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