1v7y

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(New page: 200px<br /><applet load="1v7y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v7y, resolution 2.50&Aring;" /> '''Crystal structure of...)
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[[Image:1v7y.gif|left|200px]]<br /><applet load="1v7y" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1v7y, resolution 2.50&Aring;" />
 
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'''Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli at room temperature'''<br />
 
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==Overview==
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==Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli at room temperature==
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When the tryptophan synthase alpha- and beta(2)-subunits combine to form, the alpha(2)beta(2)-complex, the enzymatic activity of each subunit is, stimulated by 1-2 orders of magnitude. To elucidate the structural basis, of this mutual activation, it is necessary to determine the structures of, the alpha- and beta-subunits alone and together with the, alpha(2)beta(2)-complex. The crystal structures of the tryptophan synthase, alpha(2)beta(2)-complex from Salmonella typhimurium, (Stalpha(2)beta(2)-complex) have already been reported. However, the, structures of the subunit alone from mesophiles have not yet been, determined. The structure of the tryptophan synthase alpha-subunit alone, from Escherichia coli (Ecalpha-subunit) was determined by an X-ray, crystallographic analysis at 2.3 A, which is the first report on the, subunits alone from the mesophiles. The biggest difference between the, structures of the Ecalpha-subunit alone and the alpha-subunit in the, Stalpha(2)beta(2)-complex (Stalpha-subunit) was as follows. Helix 2' in, the Stalpha-subunit, including an active site residue (Asp60), was changed, to a flexible loop in the Ecalpha-subunit alone. The conversion of the, helix to a loop resulted in the collapse of the correct active site, conformation. This region is also an important part for the mutual, activation in the Stalpha(2)beta(2)-complex and interaction with the, beta-subunit. These results suggest that the formation of helix 2'that is, essential for the stimulation of the enzymatic activity of the, alpha-subunit is constructed by the induced-fit mode involved in, conformational changes upon interaction between the alpha- and, beta-subunits. This also confirms the prediction of the conformational, changes based on the thermodynamic analysis for the association between, the alpha- and beta-subunits.
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<StructureSection load='1v7y' size='340' side='right'caption='[[1v7y]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1v7y]] 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=1V7Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V7Y FirstGlance]. <br>
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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]] 2.5&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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=1v7y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v7y OCA], [https://pdbe.org/1v7y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v7y RCSB], [https://www.ebi.ac.uk/pdbsum/1v7y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v7y ProSAT], [https://www.topsan.org/Proteins/RSGI/1v7y TOPSAN]</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/v7/1v7y_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=1v7y 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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When the tryptophan synthase alpha- and beta(2)-subunits combine to form the alpha(2)beta(2)-complex, the enzymatic activity of each subunit is stimulated by 1-2 orders of magnitude. To elucidate the structural basis of this mutual activation, it is necessary to determine the structures of the alpha- and beta-subunits alone and together with the alpha(2)beta(2)-complex. The crystal structures of the tryptophan synthase alpha(2)beta(2)-complex from Salmonella typhimurium (Stalpha(2)beta(2)-complex) have already been reported. However, the structures of the subunit alone from mesophiles have not yet been determined. The structure of the tryptophan synthase alpha-subunit alone from Escherichia coli (Ecalpha-subunit) was determined by an X-ray crystallographic analysis at 2.3 A, which is the first report on the subunits alone from the mesophiles. The biggest difference between the structures of the Ecalpha-subunit alone and the alpha-subunit in the Stalpha(2)beta(2)-complex (Stalpha-subunit) was as follows. Helix 2' in the Stalpha-subunit, including an active site residue (Asp60), was changed to a flexible loop in the Ecalpha-subunit alone. The conversion of the helix to a loop resulted in the collapse of the correct active site conformation. This region is also an important part for the mutual activation in the Stalpha(2)beta(2)-complex and interaction with the beta-subunit. These results suggest that the formation of helix 2'that is essential for the stimulation of the enzymatic activity of the alpha-subunit is constructed by the induced-fit mode involved in conformational changes upon interaction between the alpha- and beta-subunits. This also confirms the prediction of the conformational changes based on the thermodynamic analysis for the association between the alpha- and beta-subunits.
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==About this Structure==
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Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone.,Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K Biochemistry. 2005 Feb 1;44(4):1184-92. PMID:15667212<ref>PMID:15667212</ref>
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1V7Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V7Y OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone., Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K, Biochemistry. 2005 Feb 1;44(4):1184-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15667212 15667212]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1v7y" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Tryptophan synthase]]
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[[Category: Ishizuka, M.]]
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[[Category: Morimoto, Y.]]
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[[Category: Nishio, K.]]
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[[Category: Ogasahara, K.]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: Tsukihara, T.]]
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[[Category: Yutani, K.]]
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[[Category: SO4]]
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[[Category: riken structural genomics/proteomics initiative]]
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[[Category: rsgi]]
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[[Category: structural genomics]]
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[[Category: tryptophan]]
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[[Category: tryptophan synthase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:30:02 2007''
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==See Also==
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*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Ishizuka M]]
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[[Category: Morimoto Y]]
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[[Category: Nishio K]]
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[[Category: Ogasahara K]]
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[[Category: Tsukihara T]]
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[[Category: Yutani K]]

Current revision

Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli at room temperature

PDB ID 1v7y

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