4hwc
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4hwc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HWC FirstGlance]. <br> | <table><tr><td colspan='2'>[[4hwc]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HWC FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 1.798Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=4hwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hwc OCA], [https://pdbe.org/4hwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hwc RCSB], [https://www.ebi.ac.uk/pdbsum/4hwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hwc 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=4hwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hwc OCA], [https://pdbe.org/4hwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hwc RCSB], [https://www.ebi.ac.uk/pdbsum/4hwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hwc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/BAG1_ARATH BAG1_ARATH] Co-chaperone that regulates diverse cellular pathways, such as programmed cell death and stress responses (By similarity). | [https://www.uniprot.org/uniprot/BAG1_ARATH BAG1_ARATH] Co-chaperone that regulates diverse cellular pathways, such as programmed cell death and stress responses (By similarity). | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The recently identified plant Bcl-2-associated athanogene (BAG) family plays an extensive role in plant programmed cell death (PCD) processes ranging from growth and development to stress responses and even cell death. In the Arabidopsis thaliana BAG (AtBAG) protein family, four members (AtBAG1-4) have a domain organization similar to that of mammalian BAG proteins. Here, crystal structures of the BAG domains (BDs) of AtBAG1-4 have been determined; they have high homology and adopt a structure comprising three short parallel alpha-helices, similar to some mammalian BAG proteins. The crystal structure of a complex of the AtBAG1 ubiquitin-like domain and BAG domain (UBD) with the Hsc70 nucleotide-binding domain (NBD) was also determined. The binding of the AtBAG1 BD to the Hsc70 NBD induces conformational change of the Hsc70 NBD to the open state and reduces the affinity of the NBD for ADP. In vivo studies showed that bag2-1 mutant plants are larger than wild-type plants when growing under normal conditions, indicating that the AtBAG proteins might regulate plant PCD and confer tolerance to stresses in plants. These structural and functional analyses indicate that the AtBAG proteins function as nucleotide-exchange factors for Hsp70/Hsc70 in A. thaliana and that the mechanism of regulation of chaperone-mediated protein folding is conserved in plants. | ||
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| - | Structural insight into plant programmed cell death mediated by BAG proteins in Arabidopsis thaliana.,Fang S, Li L, Cui B, Men S, Shen Y, Yang X Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):934-45. doi:, 10.1107/S0907444913003624. Epub 2013 May 2. PMID:23695238<ref>PMID:23695238</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4hwc" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[BAG family proteins 3D structures|BAG family proteins 3D structures]] | *[[BAG family proteins 3D structures|BAG family proteins 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Structure of ATBAG1
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