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3epm
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3epm.jpg|left|200px]] | ||
| - | < | + | ==Crystal structure of Caulobacter crescentus ThiC== |
| - | + | <StructureSection load='3epm' size='340' side='right'caption='[[3epm]], [[Resolution|resolution]] 2.79Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3epm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EPM FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HMH:4-AMINO-5-HYDROXYMETHYL-2-METHYLPYRIMIDINE'>HMH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | -- | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3epn|3epn]], [[3epo|3epo]]</div></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=3epm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3epm OCA], [https://pdbe.org/3epm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3epm RCSB], [https://www.ebi.ac.uk/pdbsum/3epm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3epm ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/THIC_CAUCR THIC_CAUCR]] Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.<ref>PMID:18953358</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/ep/3epm_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=3epm ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 4-Amino-5-hydroxymethyl-2-methylpyrimidine phosphate (HMP-P) synthase catalyzes a complex rearrangement of 5-aminoimidazole ribonucleotide (AIR) to form HMP-P, the pyrimidine moiety of thiamine phosphate. We determined the three-dimensional structures of HMP-P synthase and its complexes with the product HMP-P and a substrate analog imidazole ribotide. The structure of HMP-P synthase reveals a homodimer in which each protomer comprises three domains: an N-terminal domain with a novel fold, a central (betaalpha)(8) barrel and a disordered C-terminal domain that contains a conserved CX(2)CX(4)C motif, which is suggestive of a [4Fe-4S] cluster. Biochemical studies have confirmed that HMP-P synthase is iron sulfur cluster-dependent, that it is a new member of the radical SAM superfamily and that HMP-P and 5'-deoxyadenosine are products of the reaction. Mossbauer and EPR spectroscopy confirm the presence of one [4Fe-4S] cluster. Structural comparisons reveal that HMP-P synthase is homologous to a group of adenosylcobalamin radical enzymes. This similarity supports an evolutionary relationship between these two superfamilies. | ||
| - | + | Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily.,Chatterjee A, Li Y, Zhang Y, Grove TL, Lee M, Krebs C, Booker SJ, Begley TP, Ealick SE Nat Chem Biol. 2008 Dec;4(12):758-65. Epub 2008 Oct 26. PMID:18953358<ref>PMID:18953358</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3epm" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| - | [[Category: Begley, T P | + | __TOC__ |
| - | [[Category: Booker, S J | + | </StructureSection> |
| - | [[Category: Chatterjee, A | + | [[Category: Large Structures]] |
| - | [[Category: Ealick, S E | + | [[Category: Begley, T P]] |
| - | [[Category: Grove, T L | + | [[Category: Booker, S J]] |
| - | [[Category: Krebs, C | + | [[Category: Chatterjee, A]] |
| - | [[Category: Lee, M | + | [[Category: Ealick, S E]] |
| - | [[Category: Li, S | + | [[Category: Grove, T L]] |
| - | [[Category: Zhang, Y | + | [[Category: Krebs, C]] |
| + | [[Category: Lee, M]] | ||
| + | [[Category: Li, S]] | ||
| + | [[Category: Zhang, Y]] | ||
[[Category: Alpha-beta barrel]] | [[Category: Alpha-beta barrel]] | ||
[[Category: Biosynthetic protein]] | [[Category: Biosynthetic protein]] | ||
[[Category: Sam superfamily]] | [[Category: Sam superfamily]] | ||
[[Category: Thiamine biosynthesis]] | [[Category: Thiamine biosynthesis]] | ||
| - | |||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 29 11:03:36 2008'' | ||
Current revision
Crystal structure of Caulobacter crescentus ThiC
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