1tkc: Difference between revisions

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New page: left|200px<br /><applet load="1tkc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tkc, resolution 2.7Å" /> '''SPECIFICITY OF COENZY...
 
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[[Image:1tkc.gif|left|200px]]<br /><applet load="1tkc" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1tkc, resolution 2.7&Aring;" />
'''SPECIFICITY OF COENZYME BINDING IN THIAMIN DIPHOSPHATE DEPENDENT ENZYMES: CRYSTAL STRUCTURES OF YEAST TRANSKETOLASE IN COMPLEX WITH ANALOGS OF THIAMIN DIPHOSPHATE'''<br />


==Overview==
==SPECIFICITY OF COENZYME BINDING IN THIAMIN DIPHOSPHATE DEPENDENT ENZYMES: CRYSTAL STRUCTURES OF YEAST TRANSKETOLASE IN COMPLEX WITH ANALOGS OF THIAMIN DIPHOSPHATE==
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.
<StructureSection load='1tkc' size='340' side='right'caption='[[1tkc]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1tkc]] 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=1TKC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TKC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<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=M6T:6-METHYL-THIAMIN+DIPHOSPHATE'>M6T</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=1tkc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tkc OCA], [https://pdbe.org/1tkc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tkc RCSB], [https://www.ebi.ac.uk/pdbsum/1tkc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tkc 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/1tkc_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=1tkc ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1TKC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with CA and M6T as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TKC OCA].
*[[Transketolase 3D structures|Transketolase 3D structures]]
 
== References ==
==Reference==
<references/>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8144674 8144674]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Koenig S]]
[[Category: Transketolase]]
[[Category: Schneider G]]
[[Category: Koenig, S.]]
[[Category: Schneider, G.]]
[[Category: CA]]
[[Category: M6T]]
[[Category: transferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:20:56 2007''

Latest revision as of 11:40, 14 February 2024

SPECIFICITY OF COENZYME BINDING IN THIAMIN DIPHOSPHATE DEPENDENT ENZYMES: CRYSTAL STRUCTURES OF YEAST TRANSKETOLASE IN COMPLEX WITH ANALOGS OF THIAMIN DIPHOSPHATESPECIFICITY OF COENZYME BINDING IN THIAMIN DIPHOSPHATE DEPENDENT ENZYMES: CRYSTAL STRUCTURES OF YEAST TRANSKETOLASE IN COMPLEX WITH ANALOGS OF THIAMIN DIPHOSPHATE

Structural highlights

1tkc is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Wikner C, Meshalkina L, Nilsson U, Backstrom S, Lindqvist Y, Schneider G. His103 in yeast transketolase is required for substrate recognition and catalysis. Eur J Biochem. 1995 Nov 1;233(3):750-5. PMID:8521838

1tkc, resolution 2.70Å

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