1tkb: Difference between revisions

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-[[Image:1tkb.gif|left|200px]]
- {{Structure
+==SPECIFICITY OF COENZYME BINDING IN THIAMIN DIPHOSPHATE DEPENDENT ENZYMES: CRYSTAL STRUCTURES OF YEAST TRANSKETOLASE IN COMPLEX WITH ANALOGS OF THIAMIN DIPHOSPHATE==
-|PDB= 1tkb |SIZE=350|CAPTION= <scene name='initialview01'>1tkb</scene>, resolution 2.3&Aring;
+<StructureSection load='1tkb' size='340' side='right'caption='[[1tkb]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=N1T:1&#39;-DEAZO-THIAMIN DIPHOSPHATE'>N1T</scene>
+<table><tr><td colspan='2'>[[1tkb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TKB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TKB FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Transketolase Transketolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.1 2.2.1.1]
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=N1T:1-DEAZO-THIAMIN+DIPHOSPHATE'>N1T</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=1tkb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tkb OCA], [https://pdbe.org/1tkb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tkb RCSB], [https://www.ebi.ac.uk/pdbsum/1tkb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tkb ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TKT1_YEAST TKT1_YEAST] Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.<ref>PMID:8521838</ref>
+== 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/tk/1tkb_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=1tkb ConSurf].
+<div style="clear:both"></div>
-'''SPECIFICITY OF COENZYME BINDING IN THIAMIN DIPHOSPHATE DEPENDENT ENZYMES: CRYSTAL STRUCTURES OF YEAST TRANSKETOLASE IN COMPLEX WITH ANALOGS OF THIAMIN DIPHOSPHATE'''
+==See Also==
+*[[Transketolase 3D structures|Transketolase 3D structures]]
+== References ==
-==Overview==
+<references/>
-The three-dimensional structures of complexes of yeast apotransketolase with the coenzyme analogs 6'-methyl, N1'-pyridyl, and N3'-pyridyl thiamin diphosphate, respectively, were determined with protein crystallographic methods. All three coenzyme analogs bind to the enzyme in a fashion highly similar to the cofactor thiamin diphosphate. Thus, either one of the hydrogen bonds of the pyrimidine ring nitrogens to the protein is sufficient for proper binding and positioning of the cofactor. The lack of catalytic activity of the N3'-pyridyl analog is not due to incorrect orientation of the pyrimidine ring, but results from the absence of the hydrogen bond between the N1' nitrogen atom and the conserved residue Glu418. The structure analysis provides further evidence for the importance of this conserved interaction for enzymatic thiamin catalysis.
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-TKB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TKB OCA].
-==Reference==
-Specificity of coenzyme binding in thiamin diphosphate-dependent enzymes. Crystal structures of yeast transketolase in complex with analogs of thiamin diphosphate., Konig S, Schellenberger A, Neef H, Schneider G, J Biol Chem. 1994 Apr 8;269(14):10879-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8144674 8144674]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Single protein]]
+[[Category: Koenig S]]
-[[Category: Transketolase]]
+[[Category: Schneider G]]
-[[Category: Koenig, S.]]
-[[Category: Schneider, G.]]
-[[Category: CA]]
-[[Category: N1T]]
-[[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:45:00 2008''