Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78
Wisniewska, Magdalena ; Karlberg, Tobias LU ; Lehtiö, Lari ; Johansson, Ida LU ; Kotenyova, Tetyana ; Moche, Martin and Schüler, Herwig LU
(2010)
In PLoS ONE
5(1).
- Abstract
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... (More)
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.
(Less)
- author
- Wisniewska, Magdalena
; Karlberg, Tobias
LU
; Lehtiö, Lari
; Johansson, Ida
LU
; Kotenyova, Tetyana
; Moche, Martin
and Schüler, Herwig
LU
- publishing date
- 2010-01-11
- type
- Contribution to journal
- publication status
- published
- keywords
- Adenosine Triphosphatases/chemistry, Amino Acid Sequence, Crystallography, X-Ray, DNA, Complementary, Endoplasmic Reticulum Chaperone BiP, HSP70 Heat-Shock Proteins/chemistry, Humans, Models, Molecular, Molecular Sequence Data, Protein Conformation, Protein Isoforms/chemistry, Sequence Homology, Amino Acid
- in
- PLoS ONE
- volume
- 5
- issue
- 1
- article number
- e8625
- publisher
- Public Library of Science (PLoS)
- external identifiers
-
- pmid:20072699
- scopus:77952530199
- ISSN
- 1932-6203
- DOI
- 10.1371/journal.pone.0008625
- language
- English
- LU publication?
- no
- id
- 43dbcfff-ef5e-4576-af2d-7e51a00e0497
- date added to LUP
- 2024-11-21 18:02:06
- date last changed
- 2025-07-19 00:28:31
@article{43dbcfff-ef5e-4576-af2d-7e51a00e0497,
abstract = {{<p>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.</p>}},
author = {{Wisniewska, Magdalena and Karlberg, Tobias and Lehtiö, Lari and Johansson, Ida and Kotenyova, Tetyana and Moche, Martin and Schüler, Herwig}},
issn = {{1932-6203}},
keywords = {{Adenosine Triphosphatases/chemistry; Amino Acid Sequence; Crystallography, X-Ray; DNA, Complementary; Endoplasmic Reticulum Chaperone BiP; HSP70 Heat-Shock Proteins/chemistry; Humans; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Isoforms/chemistry; Sequence Homology, Amino Acid}},
language = {{eng}},
month = {{01}},
number = {{1}},
publisher = {{Public Library of Science (PLoS)}},
series = {{PLoS ONE}},
title = {{Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78}},
url = {{http://dx.doi.org/10.1371/journal.pone.0008625}},
doi = {{10.1371/journal.pone.0008625}},
volume = {{5}},
year = {{2010}},
}