1igs

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(New page: 200px<br /><applet load="1igs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1igs, resolution 2.0&Aring;" /> '''INDOLE-3-GLYCEROLPHOS...)
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[[Image:1igs.gif|left|200px]]<br /><applet load="1igs" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1igs, resolution 2.0&Aring;" />
 
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'''INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS AT 2.0 A RESOLUTION'''<br />
 
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==Overview==
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==INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS AT 2.0 A RESOLUTION==
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BACKGROUND: Recent efforts to understand the basis of protein stability, have focused attention on comparative studies of proteins from, hyperthermophilic and mesophilic organisms. Most work to date has been on, either oligomeric enzymes or monomers comprising more than one domain., Such studies are hampered by the need to distinguish between stabilizing, interactions acting between subunits or domains from those acting within, domains. In order to simplify the search for determinants of protein, stability we have chosen to study the monomeric enzyme indole-3-glycerol, phosphate synthase from the hyperthermophilic archaeon Sulfolobus, solfataricus (sIGPS), which grows optimally at 90 degrees C. RESULTS: The, 2.0 A crystal structure of sIGPS was determined and compared with the, known 2.0 A structure of the IGPS domain of the bifunctional enzyme from, the mesophilic bacterium Escherichia coli (eIGPS). sIGPS and eIGPS have, only 30% sequence identity, but share high structural similarity. Both are, single-domain (beta/alpha)8 barrel proteins, with one (eIGPS) or two, (sIGPS) additional helices inserted before the first beta strand. The, thermostable sIGPS has many more salt bridges than eIGPS. Several salt, bridges crosslink adjacent alpha helices or participate in triple or, quadruple salt-bridge clusters. The number of helix capping, dipole, stabilizing and hydrophobic interactions is also increased in sIGPS., CONCLUSIONS: The higher stability of sIGPS compared with eIGPS seems to be, the result of several improved interactions. These include a larger number, of salt bridges, stabilization of alpha helices and strengthening of both, polypeptide chain termini and solvent-exposed loops.
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<StructureSection load='1igs' size='340' side='right'caption='[[1igs]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1igs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IGS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IGS 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&#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=PO4:PHOSPHATE+ION'>PO4</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=1igs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1igs OCA], [https://pdbe.org/1igs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1igs RCSB], [https://www.ebi.ac.uk/pdbsum/1igs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1igs ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRPC_SACS2 TRPC_SACS2]
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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/ig/1igs_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=1igs ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1IGS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IGS OCA].
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*[[IGPS 3D structures|IGPS 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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2.0 A structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability., Hennig M, Darimont B, Sterner R, Kirschner K, Jansonius JN, Structure. 1995 Dec 15;3(12):1295-306. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8747456 8747456]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Saccharolobus solfataricus]]
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[[Category: Sulfolobus solfataricus]]
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[[Category: Darimont B]]
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[[Category: Darimont, B.]]
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[[Category: Hennig M]]
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[[Category: Hennig, M.]]
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[[Category: Jansonius JN]]
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[[Category: Jansonius, J.N.]]
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[[Category: Kirschner K]]
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[[Category: Kirschner, K.]]
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[[Category: PO4]]
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[[Category: synthase]]
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[[Category: thermostable]]
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[[Category: tim-barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:23:18 2007''
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Current revision

INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS AT 2.0 A RESOLUTION

PDB ID 1igs

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