3epm
From Proteopedia
(Difference between revisions)
m (Protected "3epm" [edit=sysop:move=sysop]) |
|||
| Line 1: | Line 1: | ||
| - | [[ | + | ==Crystal structure of Caulobacter crescentus ThiC== |
| + | <StructureSection load='3epm' size='340' side='right' caption='[[3epm]], [[Resolution|resolution]] 2.79Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3epm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EPM FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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">[[3epn|3epn]], [[3epo|3epo]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">thiC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155892 Caulobacter vibrioides])</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=3epm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3epm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3epm RCSB], [http://www.ebi.ac.uk/pdbsum/3epm PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/chain_selection.php?pdb_ID=2ata 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> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Caulobacter vibrioides]] | [[Category: Caulobacter vibrioides]] | ||
| - | [[Category: Begley, T P | + | [[Category: Begley, T P]] |
| - | [[Category: Booker, S J | + | [[Category: Booker, S J]] |
| - | [[Category: Chatterjee, A | + | [[Category: Chatterjee, A]] |
| - | [[Category: Ealick, S E | + | [[Category: Ealick, S E]] |
| - | [[Category: Grove, T L | + | [[Category: Grove, T L]] |
| - | [[Category: Krebs, C | + | [[Category: Krebs, C]] |
| - | [[Category: Lee, M | + | [[Category: Lee, M]] |
| - | [[Category: Li, S | + | [[Category: Li, S]] |
| - | [[Category: Zhang, Y | + | [[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]] | ||
Revision as of 08:43, 26 November 2014
Crystal structure of Caulobacter crescentus ThiC
| |||||||||||
