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3o10

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==Crystal structure of the HEPN domain from human sacsin==
==Crystal structure of the HEPN domain from human sacsin==
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<StructureSection load='3o10' size='340' side='right' caption='[[3o10]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='3o10' size='340' side='right'caption='[[3o10]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3o10]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O10 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O10 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3o10]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O10 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=MLI:MALONATE+ION'>MLI</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]] 1.9&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SACS, KIAA0730 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3o10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o10 OCA], [https://pdbe.org/3o10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o10 RCSB], [https://www.ebi.ac.uk/pdbsum/3o10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o10 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=3o10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o10 OCA], [http://pdbe.org/3o10 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o10 RCSB], [http://www.ebi.ac.uk/pdbsum/3o10 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o10 ProSAT]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/SACS_HUMAN SACS_HUMAN]] Defects in SACS are the cause of spastic ataxia Charlevoix-Saguenay type (SACS) [MIM:[http://omim.org/entry/270550 270550]]. It is a neurodegenerative disease characterized by early-onset cerebellar ataxia, spasticity, retinal hypermyelination, pyramidal signs, and both axonal and demyelinating neuropathy with loss of sensory nerve conduction and reduced motor conduction velocities. Other features include dysarthria, distal muscle wasting, nystagmus, defect in conjugate pursuit ocular movements, retinal striation (from prominent retinal nerves) obscuring the retinal blood vessels in places, and the frequent presence of mitral valve prolapse.<ref>PMID:10655055</ref> <ref>PMID:19529988</ref> <ref>PMID:12873855</ref> <ref>PMID:15156359</ref> <ref>PMID:14718708</ref> <ref>PMID:16007637</ref> <ref>PMID:15985586</ref> <ref>PMID:17290461</ref> <ref>PMID:18398442</ref> <ref>PMID:18484239</ref> <ref>PMID:17716690</ref> <ref>PMID:18465152</ref> <ref>PMID:20876471</ref>
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[https://www.uniprot.org/uniprot/SACS_HUMAN SACS_HUMAN] Defects in SACS are the cause of spastic ataxia Charlevoix-Saguenay type (SACS) [MIM:[https://omim.org/entry/270550 270550]. It is a neurodegenerative disease characterized by early-onset cerebellar ataxia, spasticity, retinal hypermyelination, pyramidal signs, and both axonal and demyelinating neuropathy with loss of sensory nerve conduction and reduced motor conduction velocities. Other features include dysarthria, distal muscle wasting, nystagmus, defect in conjugate pursuit ocular movements, retinal striation (from prominent retinal nerves) obscuring the retinal blood vessels in places, and the frequent presence of mitral valve prolapse.<ref>PMID:10655055</ref> <ref>PMID:19529988</ref> <ref>PMID:12873855</ref> <ref>PMID:15156359</ref> <ref>PMID:14718708</ref> <ref>PMID:16007637</ref> <ref>PMID:15985586</ref> <ref>PMID:17290461</ref> <ref>PMID:18398442</ref> <ref>PMID:18484239</ref> <ref>PMID:17716690</ref> <ref>PMID:18465152</ref> <ref>PMID:20876471</ref>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SACS_HUMAN SACS_HUMAN]] Co-chaperone which acts as a regulator of the Hsp70 chaperone machinery and may be involved in the processing of other ataxia-linked proteins.<ref>PMID:19208651</ref>
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[https://www.uniprot.org/uniprot/SACS_HUMAN SACS_HUMAN] Co-chaperone which acts as a regulator of the Hsp70 chaperone machinery and may be involved in the processing of other ataxia-linked proteins.<ref>PMID:19208651</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Sacsin is a 520-kDa protein mutated in the early-onset neurodevelopmental and neurodegenerative disease autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS). The C terminus of the protein contains an HEPN (higher eukaryotes and prokaryotes nucleotide-binding) domain of unknown function. Here, we determined the high-resolution 1.9-A crystal structure of the HEPN domain from human sacsin. The structure is composed of five parallel alpha-helices with a large loop of several short helical segments. Two HEPN protomers assemble as a dimer to form a large positively charged cavity at the dimer interface that binds GTP and other nucleotides. The crystal structure reveals that the ARSACS N4549D mutation disrupts dimerization and protein folding. This study provides novel insights into the oligomerization state of sacsin and functions that are lost in mutations that cause ARSACS.
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Structural basis of defects in the sacsin HEPN domain responsible for autosomal recessive spastic ataxia of Charlevoix-Saguenay (ARSACS).,Kozlov G, Denisov AY, Girard M, Dicaire MJ, Hamlin J, McPherson PS, Brais B, Gehring K J Biol Chem. 2011 Jun 10;286(23):20407-12. Epub 2011 Apr 20. PMID:21507954<ref>PMID:21507954</ref>
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==See Also==
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*[[DnaJ homolog 3D structures|DnaJ homolog 3D structures]]
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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 3o10" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Gehring, K]]
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[[Category: Large Structures]]
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[[Category: Kozlov, G]]
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[[Category: Gehring K]]
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[[Category: All-helical domain]]
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[[Category: Kozlov G]]
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[[Category: Chaperone]]
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[[Category: Homodimerization]]
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Current revision

Crystal structure of the HEPN domain from human sacsin

PDB ID 3o10

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