3I33

Crystal structure of the human 70kDa heat shock protein 2 (Hsp70-2) ATPase domain in complex with ADP and inorganic phosphate

Summary for 3I33

• Entry DOI: 10.2210/pdb3i33/pdb
• Related: 3FE1 3GDQ
• Descriptor: Heat shock-related 70 kDa protein 2, PHOSPHATE ION, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: protein-adp complex, atp-binding, chaperone, nucleotide-binding, phosphoprotein, stress response, structural genomics, structural genomics consortium, sgc
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 45083.79

Authors

Wisniewska, M.,Karlberg, T.,Arrowsmith, C.H.,Berglund, H.,Bountra, C.,Collins, R.,Edwards, A.M.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Johansson, A.,Johansson, I.,Kotenyova, T.,Kotzsch, A.,Nielsen, T.K.,Nordlund, P.,Nyman, T.,Moche, M.,Persson, C.,Roos, A.K.,Sagemark, J.,Schutz, P.,Siponen, M.I.,Thorsell, A.G.,Tresaugues, L.,Van den Berg, S.,Weigelt, J.,Welin, M.,Schueler, H.,Structural Genomics Consortium (SGC) (deposition date: 2009-06-30, release date: 2009-07-21, Last modification date: 2023-11-01)

Primary citation

Wisniewska, M.,Karlberg, T.,Lehtio, L.,Johansson, I.,Kotenyova, T.,Moche, M.,Schueler, 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, 5:e8625-e8625, 2010

PubMed 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 and contribute little to isoform specificity, which instead is brought about by the SBDs and by accessory proteins.

PubMed: 20072699
DOI: 10.1371/journal.pone.0008625

Experimental method

X-RAY DIFFRACTION (1.3 Å)