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| | <StructureSection load='5yz1' size='340' side='right'caption='[[5yz1]], [[Resolution|resolution]] 1.97Å' scene=''> | | <StructureSection load='5yz1' size='340' side='right'caption='[[5yz1]], [[Resolution|resolution]] 1.97Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5yz1]] is a 2 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=5YZ1 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5YZ1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5yz1]] is a 2 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=5YZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YZ1 FirstGlance]. <br> |
| - | </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>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 1.97Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ZBTB8OS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5yz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yz1 OCA], [http://pdbe.org/5yz1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yz1 RCSB], [http://www.ebi.ac.uk/pdbsum/5yz1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yz1 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=5yz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yz1 OCA], [https://pdbe.org/5yz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yz1 RCSB], [https://www.ebi.ac.uk/pdbsum/5yz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yz1 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A8K0B5_HUMAN A8K0B5_HUMAN] |
| | <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: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Duan, S Y]] | + | [[Category: Duan SY]] |
| - | [[Category: Li, J X]] | + | [[Category: Li JX]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Human rtcb]]
| + | |
| - | [[Category: Key cofacor]]
| + | |
| Structural highlights
Function
A8K0B5_HUMAN
Publication Abstract from PubMed
The human archease, hereafter named HArch, is identified as a key cofactor of the tRNA-splicing ligase complex, and a potential therapeutic target for treating nervous system injuries. However, little is known about the structural basis of HArch in tRNA maturation, mRNA splicing, and RNA repair. Here we report the crystal structures of HArch and its two mutants D51A and D178A with resolutions ranging from 1.96 A to 3.4 A. HArch is composed of an extended N-terminal protrusion domain (NTD) and one compacted C-terminal domain (CTD). Unlike previously reported homologous proteins, the NTD of the first subunit interacts with the CTD of the second one, and this interaction might be important for maintaining protein stability. Moreover, HArch interacts and colocalizes with RNA ligase RTCB in cells. Our current study reveals the atomic structure of HArch and may help us understand its function in mRNA splicing.
Crystal structure of human archease, a key cofactor of tRNA splicing ligase complex.,Duan S, Gao W, Chen Z, Li Z, Li S, Gan J, Chen X, Li J Int J Biochem Cell Biol. 2020 May;122:105744. doi: 10.1016/j.biocel.2020.105744. , Epub 2020 Mar 29. PMID:32234548[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Duan S, Gao W, Chen Z, Li Z, Li S, Gan J, Chen X, Li J. Crystal structure of human archease, a key cofactor of tRNA splicing ligase complex. Int J Biochem Cell Biol. 2020 May;122:105744. doi: 10.1016/j.biocel.2020.105744. , Epub 2020 Mar 29. PMID:32234548 doi:http://dx.doi.org/10.1016/j.biocel.2020.105744
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