1vc4
From Proteopedia
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| - | [[Image:1vc4.gif|left|200px]]<br /><applet load="1vc4" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1vc4, resolution 1.80Å" /> | ||
| - | '''Crystal Structure of Indole-3-Glycerol Phosphate Synthase (TrpC) from Thermus Thermophilus At 1.8 A Resolution'''<br /> | ||
| - | == | + | ==Crystal Structure of Indole-3-Glycerol Phosphate Synthase (TrpC) from Thermus Thermophilus At 1.8 A Resolution== |
| - | + | <StructureSection load='1vc4' size='340' side='right'caption='[[1vc4]], [[Resolution|resolution]] 1.80Å' scene=''> | |
| - | [ | + | == Structural highlights == |
| - | [ | + | <table><tr><td colspan='2'>[[1vc4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VC4 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]] 1.8Å</td></tr> | |
| - | [ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1vc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vc4 OCA], [https://pdbe.org/1vc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vc4 RCSB], [https://www.ebi.ac.uk/pdbsum/1vc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vc4 ProSAT], [https://www.topsan.org/Proteins/RSGI/1vc4 TOPSAN]</span></td></tr> | |
| - | [ | + | </table> |
| - | + | == Function == | |
| - | [[ | + | [https://www.uniprot.org/uniprot/P84126_THETH P84126_THETH] |
| - | + | == 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/vc/1vc4_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=1vc4 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The three-dimensional structure of indole-3-glycerol phosphate synthase (IGPS) from the thermophilic bacterium Thermus thermophilus HB8 (TtIGPS) has been determined at 1.8 A resolution. The structure adopts a typical (beta/alpha)(8)-barrel fold with an additional N-terminal extension of 46 residues. A detailed comparison of the crystal structure of TtIGPS with available structures of IGPS from the archaeon Sulfolobus solfataricus (SsIGPS) and the bacteria Thermotoga maritima (TmIGPS) and Escherichia coli (EcIGPS) has been performed. Although the overall folds of the proteins are the same, there are differences in amino-acid composition, structural rigidity, ionic features and stability clusters which may account for the high thermostability of the hyperthermophilic (SsIGPS and TmIGPS) and thermophilic (TtIGPS) proteins when compared with the mesophilic EcIGPS. The thermostability of IGPS seems to be established mainly by favourable interactions of charged residues, salt bridges and the spatial distribution of relatively rigid clusters of extensively interacting residues. | ||
| - | + | Structure of indole-3-glycerol phosphate synthase from Thermus thermophilus HB8: implications for thermal stability.,Bagautdinov B, Yutani K Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1054-64. doi:, 10.1107/S0907444911045264. Epub 2011 Nov 18. PMID:22120743<ref>PMID:22120743</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1vc4" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[IGPS 3D structures|IGPS 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermus thermophilus]] | ||
| + | [[Category: Bagautdinov B]] | ||
| + | [[Category: Tahirov TH]] | ||
Current revision
Crystal Structure of Indole-3-Glycerol Phosphate Synthase (TrpC) from Thermus Thermophilus At 1.8 A Resolution
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