This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2d9d

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Solution structure of the BAG domain (275-350) of BAG-family molecular chaperone regulator-5

Structural highlights

2d9d is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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]

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 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2d9d"

@@ Line 1: / Line 1: @@
 ==Solution structure of the BAG domain (275-350) of BAG-family molecular chaperone regulator-5==
-<StructureSection load='2d9d' size='340' side='right' caption='[[2d9d]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2d9d' size='340' side='right'caption='[[2d9d]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2d9d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D9D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D9D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2d9d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D9D FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAG5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2d9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d9d OCA], [http://pdbe.org/2d9d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d9d RCSB], [http://www.ebi.ac.uk/pdbsum/2d9d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2d9d ProSAT], [http://www.topsan.org/Proteins/RSGI/2d9d TOPSAN]</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=2d9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d9d OCA], [https://pdbe.org/2d9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d9d RCSB], [https://www.ebi.ac.uk/pdbsum/2d9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d9d ProSAT], [https://www.topsan.org/Proteins/RSGI/2d9d TOPSAN]</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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 20: @@
 ==See Also==
-*[[BAG protein|BAG protein]]
+*[[BAG family proteins 3D structures|BAG family proteins 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Hatta, R]]
+[[Category: Large Structures]]
-[[Category: Hayashi, F]]
+[[Category: Hatta R]]
-[[Category: Structural genomic]]
+[[Category: Hayashi F]]
-[[Category: Yokoyama, S]]
+[[Category: Yokoyama S]]
-[[Category: Yoshida, M]]
+[[Category: Yoshida M]]
-[[Category: Chaperone]]
-[[Category: National project on protein structural and functional analyse]]
-[[Category: Nppsfa]]
-[[Category: Rsgi]]
-[[Category: Triple helix bundle]]

2d9d

From Proteopedia

Current revision

Solution structure of the BAG domain (275-350) of BAG-family molecular chaperone regulator-5

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox