3jxu

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the human 70kDa heat shock protein 1A (Hsp70-1) ATPase domain in complex with ADP and inorganic phosphate

Structural highlights

3jxu is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.14Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HS71A_HUMAN In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).^[1] ^[2] ^[3]

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

The 70-kDa heat shock proteins (Hsp70) are chaperones with central roles in processes that involve polypeptide remodeling events. Hsp70 proteins consist of two major functional domains: an N-terminal nucleotide binding domain (NBD) with ATPase activity, and a C-terminal substrate binding domain (SBD). We present the first crystal structures of four human Hsp70 isoforms, those of the NBDs of HSPA1L, HSPA2, HSPA5 and HSPA6. As previously with Hsp70 family members, all four proteins crystallized in a closed cleft conformation, although a slight cleft opening through rotation of subdomain IIB was observed for the HSPA5-ADP complex. The structures presented here support the view that the NBDs of human Hsp70 function by conserved mechanisms and contribute little to isoform specificity, which instead is brought about by the SBDs and by accessory proteins. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.

Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78.,Wisniewska M, Karlberg T, Lehtio L, Johansson I, Kotenyova T, Moche M, Schuler H PLoS One. 2010 Jan 11;5(1):e8625. PMID:20072699^[4]

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

References

↑ Perez-Vargas J, Romero P, Lopez S, Arias CF. The peptide-binding and ATPase domains of recombinant hsc70 are required to interact with rotavirus and reduce its infectivity. J Virol. 2006 Apr;80(7):3322-31. PMID:16537599 doi:http://dx.doi.org/80/7/3322
↑ Liu X, Liu D, Qian D, Dai J, An Y, Jiang S, Stanley B, Yang J, Wang B, Liu X, Liu DX. Nucleophosmin (NPM1/B23) interacts with activating transcription factor 5 (ATF5) protein and promotes proteasome- and caspase-dependent ATF5 degradation in hepatocellular carcinoma cells. J Biol Chem. 2012 Jun 1;287(23):19599-609. doi: 10.1074/jbc.M112.363622. Epub, 2012 Apr 23. PMID:22528486 doi:http://dx.doi.org/10.1074/jbc.M112.363622
↑ Chen Z, Barbi J, Bu S, Yang HY, Li Z, Gao Y, Jinasena D, Fu J, Lin F, Chen C, Zhang J, Yu N, Li X, Shan Z, Nie J, Gao Z, Tian H, Li Y, Yao Z, Zheng Y, Park BV, Pan Z, Zhang J, Dang E, Li Z, Wang H, Luo W, Li L, Semenza GL, Zheng SG, Loser K, Tsun A, Greene MI, Pardoll DM, Pan F, Li B. The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3. Immunity. 2013 Aug 22;39(2):272-85. doi: 10.1016/j.immuni.2013.08.006. PMID:23973223 doi:http://dx.doi.org/10.1016/j.immuni.2013.08.006
↑ Wisniewska M, Karlberg T, Lehtio L, Johansson I, Kotenyova T, Moche M, Schuler H. Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78. PLoS One. 2010 Jan 11;5(1):e8625. PMID:20072699 doi:10.1371/journal.pone.0008625

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/3jxu"

@@ Line 3: / Line 3: @@
 <StructureSection load='3jxu' size='340' side='right'caption='[[3jxu]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3jxu]] is a 1 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=3JXU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JXU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3jxu]] is a 1 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=3JXU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JXU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.14&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3i33|3i33]], [[3gdq|3gdq]], [[3iuc|3iuc]], [[3fe1|3fe1]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=3jxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jxu OCA], [http://pdbe.org/3jxu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jxu RCSB], [http://www.ebi.ac.uk/pdbsum/3jxu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jxu 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=3jxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jxu OCA], [https://pdbe.org/3jxu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jxu RCSB], [https://www.ebi.ac.uk/pdbsum/3jxu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jxu ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/HS71A_HUMAN HS71A_HUMAN] In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223).<ref>PMID:16537599</ref> <ref>PMID:22528486</ref> <ref>PMID:23973223</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Arrowsmith, C H]]
+[[Category: Arrowsmith CH]]
-[[Category: Berg, S Van Den]]
+[[Category: Berglund H]]
-[[Category: Berglund, H]]
+[[Category: Bountra C]]
-[[Category: Bountra, C]]
+[[Category: Collins R]]
-[[Category: Collins, R]]
+[[Category: Edwards AM]]
-[[Category: Edwards, A M]]
+[[Category: Flodin S]]
-[[Category: Flodin, S]]
+[[Category: Flores A]]
-[[Category: Flores, A]]
+[[Category: Graslund S]]
-[[Category: Graslund, S]]
+[[Category: Hammarstrom M]]
-[[Category: Hammarstrom, M]]
+[[Category: Johansson A]]
-[[Category: Johansson, A]]
+[[Category: Johansson I]]
-[[Category: Johansson, I]]
+[[Category: Kallas A]]
-[[Category: Kallas, A]]
+[[Category: Karlberg T]]
-[[Category: Karlberg, T]]
+[[Category: Kotenyova T]]
-[[Category: Kotenyova, T]]
+[[Category: Kotzsch A]]
-[[Category: Kotzsch, A]]
+[[Category: Kraulis P]]
-[[Category: Kraulis, P]]
+[[Category: Markova N]]
-[[Category: Markova, N]]
+[[Category: Moche M]]
-[[Category: Moche, M]]
+[[Category: Nielsen TK]]
-[[Category: Nielsen, T K]]
+[[Category: Nordlund P]]
-[[Category: Nordlund, P]]
+[[Category: Nyman T]]
-[[Category: Nyman, T]]
+[[Category: Persson C]]
-[[Category: Persson, C]]
+[[Category: Roos AK]]
-[[Category: Roos, A K]]
+[[Category: Schuler H]]
-[[Category: Structural genomic]]
+[[Category: Schutz P]]
-[[Category: Schuler, H]]
+[[Category: Siponen MI]]
-[[Category: Schutz, P]]
+[[Category: Svensson L]]
-[[Category: Siponen, M I]]
+[[Category: Thorsell AG]]
-[[Category: Svensson, L]]
+[[Category: Tresaugues L]]
-[[Category: Thorsell, A G]]
+[[Category: Van Den Berg S]]
-[[Category: Tresaugues, L]]
+[[Category: Wahlberg E]]
-[[Category: Wahlberg, E]]
+[[Category: Weigelt J]]
-[[Category: Weigelt, J]]
+[[Category: Welin M]]
-[[Category: Welin, M]]
+[[Category: Wisniewska MM]]
-[[Category: Wisniewska, M M]]
-[[Category: Atp-binding]]
-[[Category: Chaperone]]
-[[Category: Helix]]
-[[Category: Nucleotide-binding]]
-[[Category: Phosphoprotein]]
-[[Category: Polymorphism]]
-[[Category: Sgc]]
-[[Category: Stress response]]

3jxu

From Proteopedia

Current revision

Crystal structure of the human 70kDa heat shock protein 1A (Hsp70-1) ATPase domain in complex with ADP and inorganic phosphate

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox