1esj

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(New page: 200px<br /><applet load="1esj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1esj, resolution 1.80&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1esj.jpg|left|200px]]<br /><applet load="1esj" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1esj, resolution 1.80&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THIAZOLE KINASE MUTANT (C198S)'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THIAZOLE KINASE MUTANT (C198S)==
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4-Methyl-5-beta-hydroxyethylthiazole kinase (ThiK) catalyzes the, phosphorylation of the hydroxyl group of, 4-methyl-5-beta-hydroxyethylthiazole (Thz). This enzyme is a salvage, enzyme in the thiamin biosynthetic pathway and enables the cell to use, recycled Thz as an alternative to its synthesis from, 1-deoxy-D-xylulose-5-phosphate, cysteine, and tyrosine. The structure of, ThiK in the rhombohedral crystal form has been determined to 1.5 A, resolution and refined to a final R-factor of 21. 6% (R-free 25.1%). The, structures of the enzyme/Thz complex and the enzyme/Thz-phosphate/ATP, complex have also been determined. ThiK is a trimer of identical subunits., Each subunit contains a large nine-stranded central beta-sheet flanked by, helices. The overall fold is similar to that of ribokinase and adenosine, kinase, although sequence similarity is not immediately apparent. The area, of greatest similarity occurs in the ATP-binding site where several key, residues are highly conserved. Unlike adenosine kinase and ribokinase, in, which the active site is located between two domains within a single, subunit, the ThiK active site it formed at the interface between two, subunits within the trimer. The structure of the enzyme/ATP/Thz-phosphate, complex suggests that phosphate transfer occurs by an inline mechanism., Although this mechanism is similar to that proposed for both ribokinase, and adenosine kinase, ThiK lacks an absolutely conserved Asp thought to be, important for catalysis in the other two enzymes. Instead, ThiK has a, conserved cysteine (Cys198) in this position. When this Cys is mutated to, Asp, the enzymatic activity increases 10-fold. Further sequence analysis, suggests that another thiamin biosynthetic enzyme (ThiD), which catalyzes, the formation of 2-methyl-4-amino-5-hydroxymethylpyrimidine pyrophosphate, by two sequential phosphorylation reactions, belongs to the same family of, small molecule kinases.
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<StructureSection load='1esj' size='340' side='right'caption='[[1esj]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1esj]] is a 3 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=1ESJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ESJ FirstGlance]. <br>
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1ESJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Hydroxyethylthiazole_kinase Hydroxyethylthiazole kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.50 2.7.1.50] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ESJ OCA].
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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]] 1.8&#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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==Reference==
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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=1esj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esj OCA], [https://pdbe.org/1esj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1esj RCSB], [https://www.ebi.ac.uk/pdbsum/1esj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1esj ProSAT]</span></td></tr>
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Crystal structure of 4-methyl-5-beta-hydroxyethylthiazole kinase from Bacillus subtilis at 1.5 A resolution., Campobasso N, Mathews II, Begley TP, Ealick SE, Biochemistry. 2000 Jul 11;39(27):7868-77. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10891066 10891066]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/THIM_BACSU THIM_BACSU]
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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/es/1esj_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=1esj ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: Hydroxyethylthiazole kinase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Begley TP]]
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[[Category: Begley, T.P.]]
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[[Category: Campobasso N]]
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[[Category: Campobasso, N.]]
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[[Category: Ealick SE]]
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[[Category: Ealick, S.E.]]
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[[Category: Mathews II]]
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[[Category: Mathews, I.I.]]
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[[Category: SO4]]
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[[Category: alpha-beta protein]]
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[[Category: trimer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:16:47 2007''
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Current revision

CRYSTAL STRUCTURE OF THIAZOLE KINASE MUTANT (C198S)

PDB ID 1esj

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