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| | <StructureSection load='6sr6' size='340' side='right'caption='[[6sr6]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='6sr6' size='340' side='right'caption='[[6sr6]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6sr6]] is a 4 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=6SR6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6SR6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6sr6]] is a 4 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=6SR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SR6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5mb9|5mb9]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0008010 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD]), CTHT_0006310 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</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=6sr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sr6 OCA], [https://pdbe.org/6sr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sr6 RCSB], [https://www.ebi.ac.uk/pdbsum/6sr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sr6 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=6sr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sr6 OCA], [http://pdbe.org/6sr6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6sr6 RCSB], [http://www.ebi.ac.uk/pdbsum/6sr6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6sr6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G0RZX9_CHATD G0RZX9_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: Gese, G Valentin]]
| + | [[Category: Kopp J]] |
| - | [[Category: Kopp, J]] | + | [[Category: Lapouge K]] |
| - | [[Category: Lapouge, K]] | + | [[Category: Sinning I]] |
| - | [[Category: Sinning, I]] | + | [[Category: Valentin Gese G]] |
| - | [[Category: Chaperone]] | + | |
| - | [[Category: Hsp70]]
| + | |
| Structural highlights
Function
G0RZX9_CHATD
Publication Abstract from PubMed
The conserved ribosome-associated complex (RAC) consisting of Zuo1 (Hsp40) and Ssz1 (non-canonical Hsp70) acts together with the ribosome-bound Hsp70 chaperone Ssb in de novo protein folding at the ribosomal tunnel exit. Current models suggest that the function of Ssz1 is confined to the support of Zuo1, however, it is not known whether RAC by itself serves as a chaperone for nascent chains. Here we show that, via its rudimentary substrate binding domain (SBD), Ssz1 directly binds to emerging nascent chains prior to Ssb. Structural and biochemical analyses identify a conserved LP-motif at the Zuo1 N-terminus forming a polyproline-II helix, which binds to the Ssz1-SBD as a pseudo-substrate. The LP-motif competes with nascent chain binding to the Ssz1-SBD and modulates nascent chain transfer. The combined data indicate that Ssz1 is an active chaperone optimized for transient, low-affinity substrate binding, which ensures the flux of nascent chains through RAC/Ssb.
The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb.,Zhang Y, Valentin Gese G, Conz C, Lapouge K, Kopp J, Wolfle T, Rospert S, Sinning I Nat Commun. 2020 Mar 20;11(1):1504. doi: 10.1038/s41467-020-15313-w. PMID:32198371[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang Y, Valentin Gese G, Conz C, Lapouge K, Kopp J, Wolfle T, Rospert S, Sinning I. The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb. Nat Commun. 2020 Mar 20;11(1):1504. doi: 10.1038/s41467-020-15313-w. PMID:32198371 doi:http://dx.doi.org/10.1038/s41467-020-15313-w
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