1xc4

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[[Image:1xc4.png|left|200px]]
 
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==Crystal structure of wild-type tryptophan synthase alpha-subunits from Escherichia coli==
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The line below this paragraph, containing "STRUCTURE_1xc4", creates the "Structure Box" on the page.
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<StructureSection load='1xc4' size='340' side='right'caption='[[1xc4]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1xc4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XC4 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1xc4| PDB=1xc4 | SCENE= }}
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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=1xc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xc4 OCA], [https://pdbe.org/1xc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xc4 RCSB], [https://www.ebi.ac.uk/pdbsum/1xc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xc4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRPA_ECOLI TRPA_ECOLI] 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/xc/1xc4_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=1xc4 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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The alpha-subunit of tryptophan synthase (alphaTS) catalyzes the cleavage of indole-3-glycerol phosphate to glyceraldehyde-3-phosphate and indole, which is used to yield the amino acid tryptophan in tryptophan biosynthesis. Here, we report the first crystal structures of wild-type and double-mutant P28L/Y173F alpha-subunit of tryptophan synthase from Escherichia coli at 2.8 and 1.8A resolution, respectively. The structure of wild-type alphaTS from E. coli was similar to that of the alpha(2)beta(2) complex structure from Salmonella typhimurium. As compared with both structures, the conformational changes are mostly in the interface of alpha- and beta-subunits, and the substrate binding region. Two sulfate ions and two glycerol molecules per asymmetric unit bind with the residues in the active sites of the wild-type structure. Contrarily, double-mutant P28L/Y173F structure is highly closed at the window for the substrate binding by the conformational changes. The P28L substitution induces the exposure of hydrophobic amino acids and decreases the secondary structure that causes the aggregation. The Y173F suppresses to transfer a signal from the alpha-subunit core to the alpha-subunit surface involved in interactions with the beta-subunit and increases structural stability.
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===Crystal structure of wild-type tryptophan synthase alpha-subunits from Escherichia coli===
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Structures of wild-type and P28L/Y173F tryptophan synthase alpha-subunits from Escherichia coli.,Jeong MS, Jeong JK, Lim WK, Jang SB Biochem Biophys Res Commun. 2004 Oct 29;323(4):1257-64. PMID:15451433<ref>PMID:15451433</ref>
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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 1xc4" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_15451433}}, adds the Publication Abstract to the page
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*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 15451433 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15451433}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[1xc4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XC4 OCA].
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==Reference==
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<ref group="xtra">PMID:15451433</ref><ref group="xtra">PMID:3053720</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Tryptophan synthase]]
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[[Category: Large Structures]]
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[[Category: Jang, S B.]]
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[[Category: Jang SB]]
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[[Category: A-subunit]]
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[[Category: E coli]]
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[[Category: Lyase]]
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[[Category: Tryptophan synthase]]
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[[Category: Wild-type]]
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Current revision

Crystal structure of wild-type tryptophan synthase alpha-subunits from Escherichia coli

PDB ID 1xc4

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