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| | <StructureSection load='5o9e' size='340' side='right'caption='[[5o9e]], [[Resolution|resolution]] 1.88Å' scene=''> | | <StructureSection load='5o9e' size='340' side='right'caption='[[5o9e]], [[Resolution|resolution]] 1.88Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5o9e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chatd Chatd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O9E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O9E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5o9e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O9E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.884Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0062900 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD]), CTHT_0046030 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=5o9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o9e OCA], [http://pdbe.org/5o9e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o9e RCSB], [http://www.ebi.ac.uk/pdbsum/5o9e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o9e ProSAT]</span></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=5o9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o9e OCA], [https://pdbe.org/5o9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o9e RCSB], [https://www.ebi.ac.uk/pdbsum/5o9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o9e ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G0SE90_CHATD G0SE90_CHATD] |
| | <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: Chatd]] | + | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ahmed, Y L]] | + | [[Category: Ahmed YL]] |
| - | [[Category: Kharde, S]] | + | [[Category: Kharde S]] |
| - | [[Category: Sinning, I]] | + | [[Category: Sinning I]] |
| - | [[Category: Brix]]
| + | |
| - | [[Category: Ribosome]]
| + | |
| - | [[Category: Ribosome biogenesis]]
| + | |
| Structural highlights
Function
G0SE90_CHATD
Publication Abstract from PubMed
In eukaryotes, ribosome assembly is a highly complex process that involves more than 200 assembly factors that ensure the folding, modification and processing of the different rRNA species as well as the timely association of ribosomal proteins. One of these factors, Mpp10 associates with Imp3 and Imp4 to form a complex that is essential for the normal production of the 18S rRNA. Here we report the crystal structure of a complex between Imp4 and a short helical element of Mpp10 to a resolution of 1.88 A. Furthermore, we extend the interaction network of Mpp10 and characterize two novel interactions. Mpp10 is able to bind the ribosome biogenesis factor Utp3/Sas10 through two conserved motifs in its N-terminal region. In addition, Mpp10 interacts with the ribosomal protein S5/uS7 using a short stretch within an acidic loop region. Thus, our findings reveal that Mpp10 provides a platform for the simultaneous interaction with multiple proteins in the 90S pre-ribosome.
Mpp10 represents a platform for the interaction of multiple factors within the 90S pre-ribosome.,Sa-Moura B, Kornprobst M, Kharde S, Ahmed YL, Stier G, Kunze R, Sinning I, Hurt E PLoS One. 2017 Aug 16;12(8):e0183272. doi: 10.1371/journal.pone.0183272., eCollection 2017. PMID:28813493[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sa-Moura B, Kornprobst M, Kharde S, Ahmed YL, Stier G, Kunze R, Sinning I, Hurt E. Mpp10 represents a platform for the interaction of multiple factors within the 90S pre-ribosome. PLoS One. 2017 Aug 16;12(8):e0183272. doi: 10.1371/journal.pone.0183272., eCollection 2017. PMID:28813493 doi:http://dx.doi.org/10.1371/journal.pone.0183272
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