1rp0
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='1rp0' size='340' side='right'caption='[[1rp0]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1rp0' size='340' side='right'caption='[[1rp0]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1rp0]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1rp0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RP0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RP0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AHZ:ADENOSINE+DIPHOSPHATE+5-(BETA-ETHYL)-4-METHYL-THIAZOLE-2-CARBOXYLIC+ACID'>AHZ</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AHZ:ADENOSINE+DIPHOSPHATE+5-(BETA-ETHYL)-4-METHYL-THIAZOLE-2-CARBOXYLIC+ACID'>AHZ</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rp0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rp0 OCA], [https://pdbe.org/1rp0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rp0 RCSB], [https://www.ebi.ac.uk/pdbsum/1rp0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rp0 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/THI4_ARATH THI4_ARATH] Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance.<ref>PMID:8790291</ref> <ref>PMID:12941878</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 20: | Line 20: | ||
</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=1rp0 ConSurf]. | </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=1rp0 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Thiamin pyrophosphate is an essential coenzyme in all organisms that depend on fermentation, respiration or photosynthesis to produce ATP. It is synthesized through two independent biosynthetic routes: one for the synthesis of 2-methyl-4-amino-5-hydroxymethylpyrimidine pyrophosphate (pyrimidine moiety) and another for the synthesis of 4-methyl-5-(beta-hydroxyethyl) thiazole phosphate (thiazole moiety). Herein, we will describe the three-dimensional structure of THI1 protein from Arabidopsis thaliana determined by single wavelength anomalous diffraction to 1.6A resolution. The protein was produced using heterologous expression in bacteria, unexpectedly bound to 2-carboxylate-4-methyl-5-beta-(ethyl adenosine 5-diphosphate) thiazole, a potential intermediate of the thiazole biosynthesis in Eukaryotes. THI1 has a topology similar to dinucleotide binding domains and although details concerning its function are unknown, this work provides new clues about the thiazole biosynthesis in Eukaryotes. | ||
| - | |||
| - | Structure of the thiazole biosynthetic enzyme THI1 from Arabidopsis thaliana.,Godoi PH, Galhardo RS, Luche DD, Van Sluys MA, Menck CF, Oliva G J Biol Chem. 2006 Oct 13;281(41):30957-66. Epub 2006 Aug 15. PMID:16912043<ref>PMID:16912043</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1rp0" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Arabidopsis thaliana]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Godoi | + | [[Category: Godoi PHC]] |
| - | [[Category: Menck | + | [[Category: Menck CFM]] |
| - | [[Category: Oliva | + | [[Category: Oliva G]] |
| - | [[Category: Sluys | + | [[Category: Van Sluys MA]] |
| - | + | ||
| - | + | ||
Current revision
Crystal Structure of Thi1 protein from Arabidopsis thaliana
| |||||||||||
