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4gni

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==Structure of the Ssz1 ATPase bound to ATP and Magnesium==
==Structure of the Ssz1 ATPase bound to ATP and Magnesium==
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<StructureSection load='4gni' size='340' side='right' caption='[[4gni]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='4gni' size='340' side='right'caption='[[4gni]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4gni]] 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=4GNI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GNI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4gni]] 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=4GNI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GNI FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.796&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gmq|4gmq]]</td></tr>
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<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>
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<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])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gni OCA], [https://pdbe.org/4gni PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gni RCSB], [https://www.ebi.ac.uk/pdbsum/4gni PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gni ProSAT]</span></td></tr>
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<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=4gni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gni OCA], [http://pdbe.org/4gni PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gni RCSB], [http://www.ebi.ac.uk/pdbsum/4gni PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gni ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/G0RZX9_CHATD G0RZX9_CHATD]
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Ribosome-associated chaperones act in early folding events during protein synthesis. Structural information is available for prokaryotic chaperones (such as trigger factor), but structural understanding of these processes in eukaryotes lags far behind. Here we present structural analyses of the eukaryotic ribosome-associated complex (RAC) from Saccharomyces cerevisiae and Chaetomium thermophilum, consisting of heat-shock protein 70 (Hsp70) Ssz1 and the Hsp40 Zuo1. RAC is an elongated complex that crouches over the ribosomal tunnel exit and seems to be stabilized in a distinct conformation by expansion segment ES27. A unique alpha-helical domain in Zuo1 mediates ribosome interaction of RAC near the ribosomal proteins L22e and L31e and ribosomal RNA helix H59. The crystal structure of the Ssz1 ATPase domain bound to ATP-Mg(2+) explains its catalytic inactivity and suggests that Ssz1 may act before the RAC-associated chaperone Ssb. Our study offers insights into the interplay between RAC, the ER membrane-integrated Hsp40-type protein ERj1 and the signal-recognition particle.
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Structural characterization of a eukaryotic chaperone-the ribosome-associated complex.,Leidig C, Bange G, Kopp J, Amlacher S, Aravind A, Wickles S, Witte G, Hurt E, Beckmann R, Sinning I Nat Struct Mol Biol. 2012 Dec 2. doi: 10.1038/nsmb.2447. PMID:23202586<ref>PMID:23202586</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4gni" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chatd]]
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[[Category: Chaetomium thermophilum var. thermophilum DSM 1495]]
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[[Category: Bange, G]]
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[[Category: Large Structures]]
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[[Category: Sinning, I]]
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[[Category: Bange G]]
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[[Category: Atp binding protein]]
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[[Category: Sinning I]]
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[[Category: Chaperone]]
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[[Category: Co-translational chaperone]]
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[[Category: Hsp70-type atpase]]
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[[Category: Magnesium binding]]
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[[Category: Rac]]
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[[Category: Ribosome-associated complex]]
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Current revision

Structure of the Ssz1 ATPase bound to ATP and Magnesium

PDB ID 4gni

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