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| [[Image:2e09.jpg|left|200px]]<br /><applet load="2e09" size="350" color="white" frame="true" align="right" spinBox="true"
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| caption="2e09, resolution 2.40Å" />
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| '''Structure of mutant tryptophan synthase alpha-subunit (E74A) from a hyperthermophile, Pyrococcus furiosus'''<br />
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| ==Overview== | | ==Structure of mutant tryptophan synthase alpha-subunit (E74A) from a hyperthermophile, Pyrococcus furiosus== |
| The structure of the tryptophan synthase alpha-subunit from Pyrococcus furiosus was determined by x-ray analysis at 2.0-A resolution, and its stability was examined by differential scanning calorimetry. Although the structure of the tryptophan synthase alpha(2)beta(2) complex from Salmonella typhimurium has been already determined, this is the first report of the structure of the alpha-subunit alone. The alpha-subunit from P. furiosus (Pf-alpha-subunit) lacked 12 and 6 residues at the N and C termini, respectively, and one residue each in two loop regions as compared with that from S. typhimurium (St-alpha-subunit), resulting in the absence of an N-terminal helix and the shortening of a C-terminal helix. The structure of the Pf-alpha-subunit was essentially similar to that of the St-alpha-subunit in the alpha(2)beta(2) complex. The differences between both structures were discussed in connection with the higher stability of the Pf-alpha-subunit and the complex formation of the alpha- and beta-subunits. Calorimetric results indicated that the Pf-alpha-subunit has extremely high thermostability and that its higher stability is caused by an entropic effect. On the basis of structural information of both proteins, we analyzed the contributions of each stabilization factor and could conclude that hydrophobic interactions in the protein interior do not contribute to the higher stability of the Pf-alpha-subunit. Rather, the increase in ion pairs, decrease in cavity volume, and entropic effects due to shortening of the polypeptide chain play important roles in extremely high stability in Pf-alpha-subunit.
| | <StructureSection load='2e09' size='340' side='right'caption='[[2e09]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == |
| | <table><tr><td colspan='2'>[[2e09]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E09 FirstGlance]. <br> |
| | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e09 OCA], [https://pdbe.org/2e09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e09 RCSB], [https://www.ebi.ac.uk/pdbsum/2e09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e09 ProSAT], [https://www.topsan.org/Proteins/RSGI/2e09 TOPSAN]</span></td></tr> |
| | </table> |
| | == Function == |
| | [https://www.uniprot.org/uniprot/TRPA_PYRFU TRPA_PYRFU] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. |
| | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> |
| | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e0/2e09_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> |
| | </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=2e09 ConSurf]. |
| | <div style="clear:both"></div> |
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| ==About this Structure== | | ==See Also== |
| 2E09 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2E09 OCA].
| | *[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]] |
| | | __TOC__ |
| ==Reference==
| | </StructureSection> |
| Entropic stabilization of the tryptophan synthase alpha-subunit from a hyperthermophile, Pyrococcus furiosus. X-ray analysis and calorimetry., Yamagata Y, Ogasahara K, Hioki Y, Lee SJ, Nakagawa A, Nakamura H, Ishida M, Kuramitsu S, Yutani K, J Biol Chem. 2001 Apr 6;276(14):11062-71. Epub 2000 Dec 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11118452 11118452]
| | [[Category: Large Structures]] |
| [[Category: Pyrococcus furiosus]] | | [[Category: Pyrococcus furiosus]] |
| [[Category: Single protein]]
| | [[Category: Ogasahara K]] |
| [[Category: Tryptophan synthase]]
| | [[Category: Yamagata Y]] |
| [[Category: Ogasahara, K.]] | | [[Category: Yutani K]] |
| [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
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| [[Category: Yamagata, Y.]] | |
| [[Category: Yutani, K.]] | |
| [[Category: calorimetry]]
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| [[Category: hyperthermophile]]
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| [[Category: lyase]]
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| [[Category: national project on protein structural and functional analyses]]
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| [[Category: nppsfa]]
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| [[Category: pyrococcus furiosus]]
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| [[Category: riken structural genomics/proteomics initiative]]
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| [[Category: rsgi]]
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| [[Category: stability]]
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| [[Category: structural genomics]]
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| [[Category: tryptophan synthase alpha-subunit]]
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| [[Category: x-ray analysis]]
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| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:04:33 2008''
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