3epm: Difference between revisions
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==Crystal structure of Caulobacter crescentus ThiC== | ==Crystal structure of Caulobacter crescentus ThiC== | ||
<StructureSection load='3epm' size='340' side='right' caption='[[3epm]], [[Resolution|resolution]] 2.79Å' scene=''> | <StructureSection load='3epm' size='340' side='right'caption='[[3epm]], [[Resolution|resolution]] 2.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3epm]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3epm]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3EPM FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.793Å</td></tr> | ||
<tr id=' | <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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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'>[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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/THIC_CAUVC THIC_CAUVC] 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ep/3epm_consurf.spt"</scriptWhenChecked> | <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/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Caulobacter vibrioides]] | [[Category: Caulobacter vibrioides]] | ||
[[Category: Begley | [[Category: Large Structures]] | ||
[[Category: Booker | [[Category: Begley TP]] | ||
[[Category: Chatterjee | [[Category: Booker SJ]] | ||
[[Category: Ealick | [[Category: Chatterjee A]] | ||
[[Category: Grove | [[Category: Ealick SE]] | ||
[[Category: Krebs | [[Category: Grove TL]] | ||
[[Category: Lee | [[Category: Krebs C]] | ||
[[Category: Li | [[Category: Lee M]] | ||
[[Category: Zhang | [[Category: Li S]] | ||
[[Category: Zhang Y]] | |||
Latest revision as of 12:05, 30 October 2024
Crystal structure of Caulobacter crescentus ThiCCrystal structure of Caulobacter crescentus ThiC
Structural highlights
FunctionTHIC_CAUVC 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.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed4-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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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