3nl5

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<StructureSection load='3nl5' size='340' side='right'caption='[[3nl5]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='3nl5' size='340' side='right'caption='[[3nl5]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3nl5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_2001 Atcc 2001]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NL5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3nl5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_glabrata Candida glabrata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NL5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NL5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TZE:2-(4-METHYL-THIAZOL-5-YL)-ETHANOL'>TZE</scene></td></tr>
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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]] 3.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3nl2|3nl2]], [[3nl3|3nl3]], [[3nl6|3nl6]], [[3nm1|3nm1]], [[3nm3|3nm3]]</div></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=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TZE:2-(4-METHYL-THIAZOL-5-YL)-ETHANOL'>TZE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CAGL0E05808g, THI6 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5478 ATCC 2001])</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=3nl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nl5 OCA], [https://pdbe.org/3nl5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nl5 RCSB], [https://www.ebi.ac.uk/pdbsum/3nl5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nl5 ProSAT]</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=3nl5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nl5 OCA], [https://pdbe.org/3nl5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nl5 RCSB], [https://www.ebi.ac.uk/pdbsum/3nl5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nl5 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q6FV03_CANGA Q6FV03_CANGA]
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THI6 is a bifunctional enzyme found in the thiamin biosynthetic pathway in eukaryotes. The N-terminal domain of THI6 catalyzes the ligation of the thiamin thiazole and pyrimidine moieties to form thiamin phosphate, and the C-terminal domain catalyzes the phosphorylation of 4-methyl-5-hydroxyethylthiazole in a salvage pathway. In prokaryotes, thiamin phosphate synthase and 4-methyl-5-hydroxyethylthiazole kinase are separate gene products. Here we report the first crystal structure of a eukaryotic THI6 along with several complexes that characterize the active sites responsible for the two chemical reactions. THI6 from Candida glabrata is a homohexamer in which the six protomers form a cage-like structure. Each protomer is composed of two domains, which are structurally homologous to their monofunctional bacterial counterparts. Two loop regions not found in the bacterial enzymes provide interactions between the two domains. The structures of different protein-ligand complexes define the thiazole and ATP binding sites of the 4-methyl-5-hydroxyethylthiazole kinase domain and the thiazole phosphate and 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate binding sites of the thiamin phosphate synthase domain. Our structural studies reveal that the active sites of the two domains are 40 A apart and are not connected by an obvious channel. Biochemical studies show 4-methyl-5-hydroxyethylthiazole phosphate is a substrate for THI6; however, adenosine diphospho-5beta-ethyl-4-methylthiazole-2-carboxylic acid, the product of THI4, is not a substrate for THI6. This suggests that an unidentified enzyme is necessary to produce the substrate for THI6 from the THI4 product.
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Domain Organization in Candida glabrata THI6, a Bifunctional Enzyme Required for Thiamin Biosynthesis in Eukaryotes .,Paul D, Chatterjee A, Begley TP, Ealick SE Biochemistry. 2010 Nov 16;49(45):9922-34. Epub 2010 Oct 22. PMID:20968298<ref>PMID:20968298</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3nl5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 2001]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Begley, T P]]
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[[Category: Begley TP]]
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[[Category: Chatterjee, A]]
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[[Category: Chatterjee A]]
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[[Category: Ealick, S E]]
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[[Category: Ealick SE]]
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[[Category: Paul, D]]
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[[Category: Paul D]]
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[[Category: Bifunctional enzyme]]
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[[Category: Eukaryoye]]
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[[Category: Thi6]]
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[[Category: Thiamin biosynthesis]]
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[[Category: Transferase]]
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Current revision

The Crystal Structure of Candida glabrata THI6, a Bifunctional Enzyme involved in Thiamin Biosyhthesis of Eukaryotes

PDB ID 3nl5

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