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| | ==Structure of the inositol-1-phosphate CTP transferase from T. maritima.== | | ==Structure of the inositol-1-phosphate CTP transferase from T. maritima.== |
| - | <StructureSection load='4jd0' size='340' side='right' caption='[[4jd0]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='4jd0' size='340' side='right'caption='[[4jd0]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4jd0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JD0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JD0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4jd0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JD0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1KH:ARSENORIBOSE'>1KH</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1KH:ARSENORIBOSE'>1KH</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ThemaDRAFT_0946, TM1418A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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=4jd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jd0 OCA], [https://pdbe.org/4jd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jd0 RCSB], [https://www.ebi.ac.uk/pdbsum/4jd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jd0 ProSAT]</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=4jd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jd0 OCA], [http://pdbe.org/4jd0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jd0 RCSB], [http://www.ebi.ac.uk/pdbsum/4jd0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jd0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G4FFF4_THEMA G4FFF4_THEMA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Thema]] | + | [[Category: Large Structures]] |
| - | [[Category: Stec, B]] | + | [[Category: Thermotoga maritima MSB8]] |
| - | [[Category: Alpha/beta motif of sugar nucleotidyltransferase]] | + | [[Category: Stec B]] |
| - | [[Category: Transferase]]
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| Structural highlights
Function
G4FFF4_THEMA
Publication Abstract from PubMed
The unique steps in the synthesis of an unusual osmolyte in hyperthermophiles, di-myo-inositol-1,1'-phosphate (DIP), involve the production of CDP-inositol and its condensation with an inositol-1-phosphate molecule to form phosphorylated DIP. While many organisms fuse both activities into a single enzyme, the two are separate in Thermotoga maritima. The crystal structure of the T. maritima inositol-1-phosphate cytidylyltransferase, which as a soluble protein may transiently associate with its membrane-embedded partner phospho-DIP synthase (P-DIPS), has now been obtained. The structure shows a conserved motif of sugar nucleotide transferases (COG1213) with a structurally reinforced C-terminal Cys bonded to the core of the protein. A bound arsenosugar identifies the location of the active site for inositol 1-phosphate. Based on homologous structures from several species and the identification of the crucial conserved aspartate residue, a catalytic mechanism for this enzyme is proposed as well as a mode for its association with P-DIPS. This structure imposes constraints on the mode of association, communication and temperature activation of two separate enzymes in T. maritima. For the first time, a working model for the membrane-bound P-DIPS unit has been constructed. This sheds light on the functioning of the phosphatidylserine and phosphatidylinositol synthases involved in many physiological processes that are homologous to P-DIPS. This work provides fresh insights into the synthesis of the unusual thermoprotective compound DIP in hyperthermophiles.
Structure of the inositol-1-phosphate cytidylyltransferase from Thermotoga maritima.,Kurnasov OV, Luk HJ, Roberts MF, Stec B Acta Crystallogr D Biol Crystallogr. 2013 Sep 1;69(Pt 9):1808-17. doi:, 10.1107/S0907444913015278. Epub 2013 Aug 17. PMID:23999304[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kurnasov OV, Luk HJ, Roberts MF, Stec B. Structure of the inositol-1-phosphate cytidylyltransferase from Thermotoga maritima. Acta Crystallogr D Biol Crystallogr. 2013 Sep 1;69(Pt 9):1808-17. doi:, 10.1107/S0907444913015278. Epub 2013 Aug 17. PMID:23999304 doi:10.1107/S0907444913015278
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