1xqr
From Proteopedia
(New page: 200px<br /> <applet load="1xqr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xqr, resolution 2.10Å" /> '''Crystal structure o...) |
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| - | [[Image:1xqr.gif|left|200px]]<br /> | + | [[Image:1xqr.gif|left|200px]]<br /><applet load="1xqr" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1xqr, resolution 2.10Å" /> | caption="1xqr, resolution 2.10Å" /> | ||
'''Crystal structure of the HspBP1 core domain'''<br /> | '''Crystal structure of the HspBP1 core domain'''<br /> | ||
==Overview== | ==Overview== | ||
| - | HspBP1 belongs to a family of eukaryotic proteins recently identified as | + | 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== | ==About this Structure== | ||
| - | 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:// | + | 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1XQR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bracher, A.]] | [[Category: Bracher, A.]] | ||
| - | [[Category: Brodsky, J | + | [[Category: Brodsky, J L.]] |
| - | [[Category: Chang, H | + | [[Category: Chang, H C.]] |
[[Category: Dragovic, Z.]] | [[Category: Dragovic, Z.]] | ||
[[Category: Guerriero, V.]] | [[Category: Guerriero, V.]] | ||
| - | [[Category: Hartl, F | + | [[Category: Hartl, F U.]] |
[[Category: Shomura, Y.]] | [[Category: Shomura, Y.]] | ||
[[Category: Tzvetkov, N.]] | [[Category: Tzvetkov, N.]] | ||
| - | [[Category: Young, J | + | [[Category: Young, J C.]] |
[[Category: armadillo repeat]] | [[Category: armadillo repeat]] | ||
[[Category: superhelical twist]] | [[Category: superhelical twist]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:42 2008'' |
Revision as of 13:57, 21 February 2008
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Crystal structure of the HspBP1 core domain
Overview
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
1XQR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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