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Human heat shock 70kDa protein 6 (HSP70B) , ATPase domain in complex with ADP

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PDB Code 3FE1 Target Class ATPases Target HSPA6 Alias HSPA6 Disease Area/Function cancer Date Deposited Nov 27 2008 Authors Wisniewska, M., Lehtio, L., Arrowsmith, C.H., Berglund, H., Bountra, C., Collins, R., Dahlgren, L.G., Edwards, A.M., Flodin, S., Flores, A., Graslund, S., Hammarstrom, M., Johansson, A., Johansson, I., Karlberg, T., Kotenyova, T., Moche, M., Nilsson, M.E., Nordlund, P., Nyman, T., Persson, C., Sagemark, J., Siponen, M., Thorsell, A.G., Tresaugues, L., Van Den Berg, S., Weigelt, J., Welin, M., Wikstrom, M., Schueler, H.

About this structure

Heat shock-70 proteins (Hsp70) are a family of chaperones involved in the heat shock and unfolded protein response as well as housekeeping functions1. The human genome contains at least eight Hsp70 isoforms – some stress-induced, some constitutively expressed; some cytosolic and some organelle-specific. Hsp70 proteins consist of an N-terminal ATPase domain and a C-terminal peptide binding domain joined by a flexible linker. They bind extended peptide segments with a net hydrophobic character exposed during translation, membrane translocation, or following stress-induced damage, and allow refolding of such peptides. Refolding activity is coupled to ATPase activity of the N-terminal domain, which is also regulated by co-chaperones2.

The human HSPA6 protein (also called Hsp70B’) is a stress-induced member of this family that localizes to the nucleus and cytosol3-5. We determined the crystal structure of the HSPA6 ATPase domain (residues E6 – D385), which shares 85% identity with the corresponding part of the HSPA1AA (Hsp72) protein. Our structure shows the protein with one magnesium ion and the products of ATP hydrolysis (one molecule of ADP and one phosphate group) bound in the cleft between the two major lobes of the ATPase domain. Coordinates and structure factors have been deposited in the pdb (accession code 3FE1).

References

  1. Daugaard M. et al. (2007) FEBS Lett. 581, 3702-3710.
  2. Mayer M and Bukau B (2005) Cell Mol Life Sci 62, 670-684.
  3. Leung TKC et al.(1990) Biochem J 267, 125-132.
  4. Leung TKC et al.(1992) Genomics 12, 74-79.
  5. Noonan, EJ et al. (2007) Cell Stress Chaperones 12, 393-402.