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| | <StructureSection load='4y4m' size='340' side='right'caption='[[4y4m]], [[Resolution|resolution]] 2.71Å' scene=''> | | <StructureSection load='4y4m' size='340' side='right'caption='[[4y4m]], [[Resolution|resolution]] 2.71Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4y4m]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Metja Metja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y4M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y4M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4y4m]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_DSM_2661 Methanocaldococcus jannaschii DSM 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y4M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=48F:[[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]+[(2R,3R)-2,3,5-TRIS(OXIDANYL)-4-OXIDANYLIDENE-PENTYL]+HYDROGEN+PHOSPHATE'>48F</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=48F:[[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]+[(2R,3R)-2,3,5-TRIS(OXIDANYL)-4-OXIDANYLIDENE-PENTYL]+HYDROGEN+PHOSPHATE'>48F</scene>, <scene name='pdbligand=NHE:2-[N-CYCLOHEXYLAMINO]ETHANE+SULFONIC+ACID'>NHE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y4l|4y4l]], [[4y4n|4y4n]]</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=4y4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y4m OCA], [https://pdbe.org/4y4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y4m RCSB], [https://www.ebi.ac.uk/pdbsum/4y4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y4m ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MJ0601 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243232 METJA])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribose_1,5-bisphosphate_isomerase Ribose 1,5-bisphosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.29 5.3.1.29] </span></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=4y4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y4m OCA], [http://pdbe.org/4y4m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y4m RCSB], [http://www.ebi.ac.uk/pdbsum/4y4m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y4m ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RUBPS_METJA RUBPS_METJA]] Catalyzes the conversion of ribose 1,5-bisphosphate to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate for RubisCO. | + | [https://www.uniprot.org/uniprot/THI4_METJA THI4_METJA] Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur.<ref>PMID:26919468</ref> <ref>PMID:26928142</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Metja]] | + | [[Category: Methanocaldococcus jannaschii DSM 2661]] |
| - | [[Category: Ribose 1,5-bisphosphate isomerase]]
| + | [[Category: Ealick SE]] |
| - | [[Category: Ealick, S E]] | + | [[Category: Zhang X]] |
| - | [[Category: Zhang, X]] | + | |
| - | [[Category: Biosynthetic protein]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Thiazole synthase]]
| + | |
| Structural highlights
Function
THI4_METJA Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur.[1] [2]
Publication Abstract from PubMed
Thiamin diphosphate is an essential cofactor in all forms of life and plays a key role in amino acid and carbohydrate metabolism. Its biosynthesis involves separate syntheses of the pyrimidine and thiazole moieties, which are then coupled to form thiamin monophosphate. A final phosphorylation produces the active form of the cofactor. In most bacteria, six gene products are required for biosynthesis of the thiamin thiazole. In yeast and fungi only one gene product, Thi4, is required for thiazole biosynthesis. Methanococcus jannaschii expresses a putative Thi4 ortholog that was previously reported to be a ribulose 1, 5-bisphosphate synthase [Finn, M. W. and Tabita, F. R. (2004) J. Bacteriol. 186, 6360-6366]. Our structural studies show that the Thi4 orthologs from M. jannaschii and Methanococcus igneus are structurally homologous to Thi4 from Saccharomyces cerevisiae . In addition, all active site residues are conserved except for a key cysteine residue, which in S. cerevisiae is the source of the thiazole sulfur atom. Our recent biochemical studies showed that the archael Thi4 orthologs use nicotinamide adenine dinucleotide, glycine and free sulfide to form the thiamin thiazole in an iron-dependent reaction [Eser, B., Zhang, X., Chanani, P. K., Ealick, S.E., and Begley, T.P. (2015) submitted]. Here we report X-ray crystal structures of Thi4 from M. jannaschii complexed with ADP-ribulose, the C205S variant of Thi4 from S. cerevisiae with a bound glycine imine intermediate, and Thi4 from M. igneus with bound glycine imine intermediate and iron. These studies reveal the structural basis for the iron-dependent mechanism of sulfur transfer in archael and yeast thiazole synthases.
Structural Basis for Iron-mediated Sulfur Transfer in Archael and Yeast Thiazole Synthases.,Zhang X, Eser BE, Chanani PK, Begley TP, Ealick SE Biochemistry. 2016 Feb 26. PMID:26919468[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang X, Eser BE, Chanani PK, Begley TP, Ealick SE. Structural Basis for Iron-mediated Sulfur Transfer in Archael and Yeast Thiazole Synthases. Biochemistry. 2016 Feb 26. PMID:26919468 doi:http://dx.doi.org/10.1021/acs.biochem.6b00030
- ↑ Eser BE, Zhang X, Chanani PK, Begley TP, Ealick SE. From Suicide Enzyme to Catalyst: The Iron-Dependent Sulfide Transfer in Methanococcus jannaschii Thiamin Thiazole Biosynthesis. J Am Chem Soc. 2016 Mar 23;138(11):3639-42. PMID:26928142 doi:10.1021/jacs.6b00445
- ↑ Zhang X, Eser BE, Chanani PK, Begley TP, Ealick SE. Structural Basis for Iron-mediated Sulfur Transfer in Archael and Yeast Thiazole Synthases. Biochemistry. 2016 Feb 26. PMID:26919468 doi:http://dx.doi.org/10.1021/acs.biochem.6b00030
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