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1i4n

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[[Image:1i4n.gif|left|200px]]<br /><applet load="1i4n" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1i4n, resolution 2.5&Aring;" />
 
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'''CRYSTAL STRUCTURE OF INDOLEGLYCEROL PHOSPHATE SYNTHASE FROM THERMOTOGA MARITIMA'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF INDOLEGLYCEROL PHOSPHATE SYNTHASE FROM THERMOTOGA MARITIMA==
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The crystal structure of the thermostable indoleglycerol-phosphate synthase from Thermotoga maritima (tIGPS) was determined at 2.5 A resolution. It was compared with the structures of the thermostable sIGPS from Sulfolobus solfataricus and of the thermolabile eIGPS from Escherichia coli. The main chains of the three (beta alpha)(8)-barrel proteins superimpose closely, and the packing of side chains in the beta-barrel cores, as well as the architecture of surface loops, is very similar. Both thermostable proteins have, however, 17 strong salt bridges, compared with only 10 in eIGPS. The number of additional salt bridges in tIGPS and sIGPS correlates well with their reduced rate of irreversible thermal inactivation at 90 degrees C. Only 3 of 17 salt bridges in tIGPS and sIGPS are topologically conserved. The major difference between the two proteins is the preference for interhelical salt bridges in sIGPS and intrahelical ones in tIGPS. The different implementation of salt bridges in the closely related proteins suggests that the stabilizing effect of salt bridges depends rather on the sum of their individual contributions than on their location. This observation is consistent with a protein unfolding mechanism where the simultaneous breakdown of all salt bridges is the rate-determining step.
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<StructureSection load='1i4n' size='340' side='right'caption='[[1i4n]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1i4n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I4N 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=1i4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i4n OCA], [https://pdbe.org/1i4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i4n RCSB], [https://www.ebi.ac.uk/pdbsum/1i4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i4n ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRPC_THEMA TRPC_THEMA]
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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/i4/1i4n_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=1i4n 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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1I4N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Indole-3-glycerol-phosphate_synthase Indole-3-glycerol-phosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.48 4.1.1.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I4N 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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The crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridges., Knochel T, Pappenberger A, Jansonius JN, Kirschner K, J Biol Chem. 2002 Mar 8;277(10):8626-34. Epub 2001 Dec 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11741953 11741953]
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[[Category: Large Structures]]
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[[Category: Indole-3-glycerol-phosphate synthase]]
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[[Category: Single protein]]
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[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Jansonius, J N.]]
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[[Category: Jansonius JN]]
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[[Category: Kirschner, K.]]
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[[Category: Kirschner K]]
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[[Category: Knoechel, T.]]
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[[Category: Knoechel T]]
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[[Category: Pappenberger, A.]]
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[[Category: Pappenberger A]]
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[[Category: SO4]]
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[[Category: indoleglycerol phosphate synthase; thermotoga maritima; thermostable tim-barrel protein; salt bridges; electrostatic interactions]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:56 2008''
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Current revision

CRYSTAL STRUCTURE OF INDOLEGLYCEROL PHOSPHATE SYNTHASE FROM THERMOTOGA MARITIMA

PDB ID 1i4n

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