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1fnk

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(New page: 200px<br /><applet load="1fnk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fnk, resolution 2.00&Aring;" /> '''CRYSTAL STRUCTURE AN...)
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[[Image:1fnk.gif|left|200px]]<br /><applet load="1fnk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fnk, resolution 2.00&Aring;" />
 
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'''CRYSTAL STRUCTURE ANALYSIS OF CHORISMATE MUTASE MUTANT C88K/R90S'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE ANALYSIS OF CHORISMATE MUTASE MUTANT C88K/R90S==
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Combinatorial mutagenesis and in vivo selection experiments previously, afforded functional variants of the AroH class Bacillus subtilis, chorismate mutase lacking the otherwise highly conserved active site, residue Arg(90). Here, we present a detailed kinetic and crystallographic, study of several such variants. Removing the arginine side chain (R90G and, R90A) reduced catalytic efficiency by more than 5 orders of magnitude., Reintroducing a positive charge to the active site through lysine, substitutions restored more than a factor of a thousand in k(cat)., Remarkably, the lysine could be placed at position 90 or at the more, remote position 88 provided a sterically suitable residue was present at, the partner site. Crystal structures of the double mutants C88S/R90K and, C88K/R90S show that the lysine adopts an extended conformation that would, place its epsilon-ammonium group within hydrogen-bonding distance of the, ether oxygen of bound chorismate in the transition state. These results, provide support for the hypothesis that developing negative charge in the, highly polarized transition state is stabilized electrostatically by a, strategically placed cation. The implications of this finding for the, mechanism of all natural chorismate mutases and for the design of, artificial catalysts are discussed.
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<StructureSection load='1fnk' size='340' side='right'caption='[[1fnk]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1fnk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FNK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FNK 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=CSD:3-SULFINOALANINE'>CSD</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=1fnk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fnk OCA], [https://pdbe.org/1fnk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fnk RCSB], [https://www.ebi.ac.uk/pdbsum/1fnk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fnk ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AROH_BACSU AROH_BACSU] Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.<ref>PMID:2105742</ref>
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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/fn/1fnk_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=1fnk 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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1FNK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Active as [http://en.wikipedia.org/wiki/Chorismate_mutase Chorismate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.5 5.4.99.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FNK OCA].
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*[[3D structures of chorismate mutase|3D structures of chorismate mutase]]
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== References ==
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==Reference==
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<references/>
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A strategically positioned cation is crucial for efficient catalysis by chorismate mutase., Kast P, Grisostomi C, Chen IA, Li S, Krengel U, Xue Y, Hilvert D, J Biol Chem. 2000 Nov 24;275(47):36832-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10960481 10960481]
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Chorismate mutase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Chen IA]]
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[[Category: Chen, I.A.]]
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[[Category: Grisostomi C]]
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[[Category: Grisostomi, C.]]
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[[Category: Hilvert D]]
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[[Category: Hilvert, D.]]
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[[Category: Kast P]]
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[[Category: Kast, P.]]
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[[Category: Krengel U]]
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[[Category: Krengel, U.]]
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[[Category: Li S]]
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[[Category: Li, S.]]
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[[Category: Xue Y]]
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[[Category: Xue, Y.]]
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[[Category: chorismate mutase]]
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[[Category: crystal structure]]
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[[Category: mutant]]
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[[Category: protein]]
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[[Category: pseudo-alpha beta-barrel]]
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[[Category: trimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:04:05 2007''
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Current revision

CRYSTAL STRUCTURE ANALYSIS OF CHORISMATE MUTASE MUTANT C88K/R90S

PDB ID 1fnk

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