3a8y

From Proteopedia

(Difference between revisions)

Revision as of 16:19, 22 December 2021

Crystal structure of the complex between the BAG5 BD5 and Hsp70 NBD

Structural highlights

3a8y is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	Hsp70 (HUMAN), BAG5 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BAG5_HUMAN] Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 (By similarity). May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

ADP-ATP exchange by the molecular chaperone Hsp70 is enhanced by several cochaperones. BAG5 consists of five BAG domains and associates with the nucleotide-binding domain (NBD) of Hsp70. The overexpression of BAG5 in the cytosol reportedly disturbs Hsp70-mediated protein refolding and induces Parkinson's disease. In the present study, we found that the fifth BAG domain (BD5) of BAG5 is responsible for the interaction between Hsp70 and BAG5. We also determined the crystal structures of the BD5*NBD complex. BD5 binding caused two different types of NBD conformational changes, which both disrupted the nucleotide-binding groove. In fact, BD5 reduced the affinity of the NBD for ADP. Moreover, BD5, as well as the full-length BAG5, accelerated Hsp70-mediated refolding in an in vitro assay. Therefore, BAG5 can function as the nucleotide exchange factor of Hsp70 for the enhancement of protein refolding.

The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange.,Arakawa A, Handa N, Ohsawa N, Shida M, Kigawa T, Hayashi F, Shirouzu M, Yokoyama S Structure. 2010 Mar 10;18(3):309-19. PMID:20223214^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Arakawa A, Handa N, Ohsawa N, Shida M, Kigawa T, Hayashi F, Shirouzu M, Yokoyama S. The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange. Structure. 2010 Mar 10;18(3):309-19. PMID:20223214 doi:10.1016/j.str.2010.01.004
↑ Arakawa A, Handa N, Ohsawa N, Shida M, Kigawa T, Hayashi F, Shirouzu M, Yokoyama S. The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange. Structure. 2010 Mar 10;18(3):309-19. PMID:20223214 doi:10.1016/j.str.2010.01.004

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3a8y"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the complex between the BAG5 BD5 and Hsp70 NBD==
-<StructureSection load='3a8y' size='340' side='right' caption='[[3a8y]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='3a8y' size='340' side='right'caption='[[3a8y]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3a8y]] 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=3A8Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A8Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3a8y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A8Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A8Y FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hsp70 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), BAG5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hsp70 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), BAG5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-<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=3a8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8y OCA], [http://pdbe.org/3a8y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a8y RCSB], [http://www.ebi.ac.uk/pdbsum/3a8y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a8y 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=3a8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a8y OCA], [https://pdbe.org/3a8y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a8y RCSB], [https://www.ebi.ac.uk/pdbsum/3a8y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a8y ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/BAG5_HUMAN BAG5_HUMAN]] Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 (By similarity). May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding.<ref>PMID:20223214</ref>
+[[https://www.uniprot.org/uniprot/BAG5_HUMAN BAG5_HUMAN]] Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 (By similarity). May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding.<ref>PMID:20223214</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[BAG protein|BAG protein]]
+*[[BAG family proteins 3D structures|BAG family proteins 3D structures]]
-*[[Heat Shock Proteins|Heat Shock Proteins]]
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 == References ==
 <references/>
@@ Line 38: / Line 38: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Arakawa, A]]
 [[Category: Handa, N]]

3a8y

From Proteopedia

Revision as of 16:19, 22 December 2021

Crystal structure of the complex between the BAG5 BD5 and Hsp70 NBD

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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