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.


1xqr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1xqr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xqr, resolution 2.10&Aring;" /> '''Crystal structure o...)
Current revision (07:56, 15 May 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1xqr.gif|left|200px]]<br />
 
-
<applet load="1xqr" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1xqr, resolution 2.10&Aring;" />
 
-
'''Crystal structure of the HspBP1 core domain'''<br />
 
-
==Overview==
+
==Crystal structure of the HspBP1 core domain==
-
HspBP1 belongs to a family of eukaryotic proteins recently identified as, nucleotide exchange factors for Hsp70. We show that the S. cerevisiae, ortholog of HspBP1, Fes1p, is required for efficient protein folding in, the cytosol at 37 degrees C. The crystal structure of HspBP1, alone and, complexed with part of the Hsp70 ATPase domain, reveals a mechanism for, its function distinct from that of BAG-1 or GrpE, previously characterized, nucleotide exchange factors of Hsp70. HspBP1 has a curved, all, alpha-helical fold containing four armadillo-like repeats unlike the other, nucleotide exchange factors. The concave face of HspBP1 embraces lobe II, of the ATPase domain, and a steric conflict displaces lobe I, reducing the, affinity for nucleotide. In contrast, BAG-1 and GrpE trigger a conserved, conformational change in lobe II of the ATPase domain. Thus, nucleotide, exchange on eukaryotic Hsp70 occurs through two distinct mechanisms.
+
<StructureSection load='1xqr' size='340' side='right'caption='[[1xqr]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1xqr]] 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=1XQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XQR FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1xqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xqr OCA], [https://pdbe.org/1xqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xqr RCSB], [https://www.ebi.ac.uk/pdbsum/1xqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xqr ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/HPBP1_HUMAN HPBP1_HUMAN] Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR.<ref>PMID:9830037</ref> <ref>PMID:10786638</ref> <ref>PMID:12651857</ref> <ref>PMID:15215316</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xq/1xqr_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xqr ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
HspBP1 belongs to a family of eukaryotic proteins recently identified as nucleotide exchange factors for Hsp70. We show that the S. cerevisiae ortholog of HspBP1, Fes1p, is required for efficient protein folding in the cytosol at 37 degrees C. The crystal structure of HspBP1, alone and complexed with part of the Hsp70 ATPase domain, reveals a mechanism for its function distinct from that of BAG-1 or GrpE, previously characterized nucleotide exchange factors of Hsp70. HspBP1 has a curved, all alpha-helical fold containing four armadillo-like repeats unlike the other nucleotide exchange factors. The concave face of HspBP1 embraces lobe II of the ATPase domain, and a steric conflict displaces lobe I, reducing the affinity for nucleotide. In contrast, BAG-1 and GrpE trigger a conserved conformational change in lobe II of the ATPase domain. Thus, nucleotide exchange on eukaryotic Hsp70 occurs through two distinct mechanisms.
-
==About this Structure==
+
Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange.,Shomura Y, Dragovic Z, Chang HC, Tzvetkov N, Young JC, Brodsky JL, Guerriero V, Hartl FU, Bracher A Mol Cell. 2005 Feb 4;17(3):367-79. PMID:15694338<ref>PMID:15694338</ref>
-
1XQR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XQR OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange., Shomura Y, Dragovic Z, Chang HC, Tzvetkov N, Young JC, Brodsky JL, Guerriero V, Hartl FU, Bracher A, Mol Cell. 2005 Feb 4;17(3):367-79. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15694338 15694338]
+
</div>
 +
<div class="pdbe-citations 1xqr" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Bracher, A.]]
+
[[Category: Bracher A]]
-
[[Category: Brodsky, J.L.]]
+
[[Category: Brodsky JL]]
-
[[Category: Chang, H.C.]]
+
[[Category: Chang HC]]
-
[[Category: Dragovic, Z.]]
+
[[Category: Dragovic Z]]
-
[[Category: Guerriero, V.]]
+
[[Category: Guerriero V]]
-
[[Category: Hartl, F.U.]]
+
[[Category: Hartl FU]]
-
[[Category: Shomura, Y.]]
+
[[Category: Shomura Y]]
-
[[Category: Tzvetkov, N.]]
+
[[Category: Tzvetkov N]]
-
[[Category: Young, J.C.]]
+
[[Category: Young JC]]
-
[[Category: armadillo repeat]]
+
-
[[Category: superhelical twist]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:09:46 2007''
+

Current revision

Crystal structure of the HspBP1 core domain

PDB ID 1xqr

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1xqr"
Personal tools