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1kfk

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[[Image:1kfk.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of Tryptophan Synthase From Salmonella Typhimurium==
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|PDB= 1kfk |SIZE=350|CAPTION= <scene name='initialview01'>1kfk</scene>, resolution 2.40&Aring;
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<StructureSection load='1kfk' size='340' side='right'caption='[[1kfk]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
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<table><tr><td colspan='2'>[[1kfk]] 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] and [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFK FirstGlance]. <br>
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|ACTIVITY= [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]
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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]] 2.4&#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=NA:SODIUM+ION'>NA</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=1kfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfk OCA], [https://pdbe.org/1kfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfk RCSB], [https://www.ebi.ac.uk/pdbsum/1kfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfk 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/1kfk_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=1kfk ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of Tryptophan Synthase From Salmonella Typhimurium'''
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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: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]]
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1KFK is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] and [http://en.wikipedia.org/wiki/Salmonella_typhimurium_lt2 Salmonella typhimurium lt2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFK OCA].
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[[Category: Arac D]]
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[[Category: Dunn MF]]
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==Reference==
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[[Category: Kulik V]]
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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: Niks D]]
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[[Category: Protein complex]]
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[[Category: Schlichting I]]
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[[Category: Salmonella typhimurium]]
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[[Category: Seidel R]]
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[[Category: Salmonella typhimurium lt2]]
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[[Category: Weyand M]]
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[[Category: Tryptophan synthase]]
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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: Seidel, R.]]
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[[Category: Weyand, M.]]
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[[Category: NA]]
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[[Category: PLP]]
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[[Category: carbon-oxygen lyase]]
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[[Category: pyridoxal phosphate]]
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[[Category: tryptophan biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:28:53 2008''
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Current revision

Crystal structure of Tryptophan Synthase From Salmonella Typhimurium

PDB ID 1kfk

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