View source for 5v47


==Crystal structure of the SR1 domain of lizard sacsin==
<StructureSection load='5v47' size='340' side='right'caption='[[5v47]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5v47]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Anolis_carolinensis Anolis carolinensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V47 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V47 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5v47 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v47 OCA], [https://pdbe.org/5v47 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v47 RCSB], [https://www.ebi.ac.uk/pdbsum/5v47 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v47 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G1KBF9_ANOCA G1KBF9_ANOCA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS) is a neurodegenerative disease that is caused by mutations in the SACS gene. The product of this gene is a very large 520 kDa cytoplasmic protein, sacsin, with an ubiquitin-like domain (Ubl) at the N-terminus followed by three large sacsin internal repeats (SIRPTs) supradomains and C-terminal J and HEPN domains. The SIRPTs are predicted to contain Hsp90-like domains suggesting a potential chaperone activity. In this work, we report the structures of the Hsp90-like Sr1 domain of SIRPT1 and the N-terminal Ubl domain determined at 1.55 A and 2.1 A resolution, respectively. The Ubl domain crystallized as a swapped dimer that could be relevant in the context of full-length protein. The Sr1 domain displays the Bergerat protein fold with a characteristic nucleotide-binding pocket, though it binds nucleotides with very low affinity. The Sr1 structure reveals that ARSACS-causing missense mutations (R272H, R272C and T201K) disrupt protein folding most likely leading to sacsin degradation. This work lends a structural support to the view of sacsin as a molecular chaperone and provides a framework for future studies of this protein.

Structures of Ubl and Hsp90-like domains of sacsin provide insight into pathological mutations.,Menade M, Kozlov G, Trempe JF, Pande H, Shenker S, Wickremasinghe S, Li X, Hojjat H, Dicaire MJ, Brais B, McPherson PS, Wong MJH, Young JC, Gehring K J Biol Chem. 2018 Jun 26. pii: RA118.003939. doi: 10.1074/jbc.RA118.003939. PMID:29945973<ref>PMID:29945973</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5v47" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Anolis carolinensis]]
[[Category: Large Structures]]
[[Category: Gehring K]]
[[Category: Kozlov G]]
[[Category: Menade M]]
[[Category: Pan T]]