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| | <StructureSection load='4x33' size='340' side='right'caption='[[4x33]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='4x33' size='340' side='right'caption='[[4x33]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4x33]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X33 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4X33 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4x33]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X33 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DXE:1,2-DIMETHOXYETHANE'>DXE</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=DXE:1,2-DIMETHOXYETHANE'>DXE</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</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=4x33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x33 OCA], [https://pdbe.org/4x33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x33 RCSB], [https://www.ebi.ac.uk/pdbsum/4x33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x33 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KTI11, DPH3, YBL071W-A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast]), ATS1, YAL020C, FUN28, YAL006 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=4x33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x33 OCA], [http://pdbe.org/4x33 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4x33 RCSB], [http://www.ebi.ac.uk/pdbsum/4x33 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4x33 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DPH3_YEAST DPH3_YEAST]] Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2. Required for conferring sensitivity to K.lactis zymocin.<ref>PMID:15485916</ref> [[http://www.uniprot.org/uniprot/ATS1_YEAST ATS1_YEAST]] May participate in regulatory interactions between microtubules and the cell cycle. | + | [https://www.uniprot.org/uniprot/DPH3_YEAST DPH3_YEAST] Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2. Required for conferring sensitivity to K.lactis zymocin.<ref>PMID:15485916</ref> |
| | <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: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cavarelli, J]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Kolaj-Robin, O]] | + | [[Category: Cavarelli J]] |
| - | [[Category: McEwen, A G]] | + | [[Category: Kolaj-Robin O]] |
| - | [[Category: Seraphin, B]] | + | [[Category: McEwen AG]] |
| - | [[Category: Complex]]
| + | [[Category: Seraphin B]] |
| - | [[Category: Electron transfer]]
| + | |
| - | [[Category: Electron transport]]
| + | |
| - | [[Category: Trna modification]]
| + | |
| Structural highlights
Function
DPH3_YEAST Required for the first step of diphthamide biosynthesis, the transfer of 3-amino-3-carboxypropyl from S-adenosyl-L-methionine to a histidine residue. Diphthamide is a post-translational modification of histidine which occurs in elongation factor 2. Required for conferring sensitivity to K.lactis zymocin.[1]
Publication Abstract from PubMed
Modification of wobble uridines of many eukaryotic tRNAs requires the Elongator complex, a highly conserved six-subunit eukaryotic protein assembly, as well as the Killer toxin-insensitive (Kti) proteins 11-14. Kti11 was additionally shown to be implicated in the biosynthesis of diphthamide, a post-translationally modified histidine of translation elongation factor 2. Recent data indicate that iron-bearing Kti11 functions as an electron donor to the [4Fe-4S] cluster of radical S-Adenosylmethionine enzymes, triggering the subsequent radical reaction. We show here that recombinant yeast Kti11 forms a stable 1 : 1 complex with Kti13. To obtain insights into the function of this heterodimer, the Kti11/Kti13 complex was purified to homogeneity, crystallized, and its structure determined at 1.45 A resolution. The importance of several residues mediating complex formation was confirmed by mutagenesis. Kti13 adopts a fold characteristic of RCC1-like proteins. The seven-bladed beta-propeller consists of a unique mixture of four- and three-stranded blades. In the complex, Kti13 orients Kti11 and restricts access to its electron-carrying iron atom, constraining the electron transfer capacity of Kti11. Based on these findings, we propose a role for Kti13, and discuss the possible functional implications of complex formation. DATABASE: Structural data have been submitted to the Protein Data Bank under accession number 4X33.
Structure of the Elongator cofactor complex Kti11/Kti13 provides insight into the role of Kti13 in Elongator-dependent tRNA modification.,Kolaj-Robin O, McEwen AG, Cavarelli J, Seraphin B FEBS J. 2015 Jan 21. doi: 10.1111/febs.13199. PMID:25604895[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu S, Milne GT, Kuremsky JG, Fink GR, Leppla SH. Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2. Mol Cell Biol. 2004 Nov;24(21):9487-97. PMID:15485916 doi:http://dx.doi.org/10.1128/MCB.24.21.9487-9497.2004
- ↑ Kolaj-Robin O, McEwen AG, Cavarelli J, Seraphin B. Structure of the Elongator cofactor complex Kti11/Kti13 provides insight into the role of Kti13 in Elongator-dependent tRNA modification. FEBS J. 2015 Jan 21. doi: 10.1111/febs.13199. PMID:25604895 doi:http://dx.doi.org/10.1111/febs.13199
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