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| ==Structure of Trifunctional THI20 from Yeast== | | ==Structure of Trifunctional THI20 from Yeast== |
| <StructureSection load='3rm5' size='340' side='right' caption='[[3rm5]], [[Resolution|resolution]] 2.68Å' scene=''> | | <StructureSection load='3rm5' size='340' side='right'caption='[[3rm5]], [[Resolution|resolution]] 2.68Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3rm5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RM5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RM5 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3rm5]] 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=3RM5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RM5 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.68Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">O1239, THI20, Thi20p, YOL055C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | | <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> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rm5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rm5 RCSB], [http://www.ebi.ac.uk/pdbsum/3rm5 PDBsum]</span></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=3rm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rm5 OCA], [https://pdbe.org/3rm5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rm5 RCSB], [https://www.ebi.ac.uk/pdbsum/3rm5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rm5 ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
| [[http://www.uniprot.org/uniprot/THI20_YEAST THI20_YEAST]] Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and also probaby that of HMP to HMP-P. | | [https://www.uniprot.org/uniprot/THI20_YEAST THI20_YEAST] Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and also probaby that of HMP to HMP-P. |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| In a recently characterized thiamin-salvage pathway, thiamin-degradation products are hydrolyzed by thiaminase II, yielding 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP). This compound is an intermediate in thiamin biosynthesis that, once phosphorylated by an HMP kinase, can be used to synthesize thiamin monophosphate. Here, the crystal structure of Saccharomyces cerevisiae THI20, a trifunctional enzyme containing an N-terminal HMP kinase/HMP-P kinase (ThiD-like) domain and a C-terminal thiaminase II (TenA-like) domain, is presented. Comparison to structures of the monofunctional enzymes reveals that while the ThiD-like dimer observed in THI20 resembles other ThiD structures, the TenA-like domain, which is tetrameric in all previously reported structures, forms a dimer. Similarly, the active site of the ThiD-like domain of THI20 is highly similar to other known ThiD enzymes, while the TenA-like active site shows unique features compared with previously structurally characterized TenAs. In addition, a survey of known TenA structures revealed two structural classes, both of which have distinct conserved features. The TenA domain of THI20 possesses some features of both classes, consistent with its ability to hydrolyze both thiamin and the thiamin-degradation product 2-methyl-4-amino-5-aminomethylpyrimidine.
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| Structure of trifunctional THI20 from yeast.,French JB, Begley TP, Ealick SE Acta Crystallogr D Biol Crystallogr. 2011 Sep;67(Pt 9):784-91. Epub 2011, Aug 9. PMID:21904031<ref>PMID:21904031</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Atcc 18824]] | | [[Category: Large Structures]] |
| [[Category: Begley, T P]] | | [[Category: Saccharomyces cerevisiae]] |
| [[Category: Ealick, S E]] | | [[Category: Begley TP]] |
| [[Category: French, J B]] | | [[Category: Ealick SE]] |
| [[Category: Thiaminase ii]] | | [[Category: French JB]] |
| [[Category: Transferase]]
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