2Y4T
Crystal structure of the human co-chaperone P58(IPK)
Summary for 2Y4T
| Entry DOI | 10.2210/pdb2y4t/pdb |
| Related | 2Y4U |
| Descriptor | DNAJ HOMOLOG SUBFAMILY C MEMBER 3 (2 entities in total) |
| Functional Keywords | chaperone, endoplasmic reticulum, protein folding, tetratricopeptiderepeat, j domain, unfolded protein response |
| Biological source | HOMO SAPIENS (HUMAN) |
| Cellular location | Endoplasmic reticulum (By similarity): Q13217 |
| Total number of polymer chains | 3 |
| Total formula weight | 155840.51 |
| Authors | Svard, M.,Biterova, E.I.,Bourhis, J.-M.,Guy, J.E. (deposition date: 2011-01-10, release date: 2011-08-10, Last modification date: 2024-11-06) |
| Primary citation | Svard, M.,Biterova, E.I.,Bourhis, J.-M.,Guy, J.E. The Crystal Structure of the Human Co-Chaperone P58Ipk Plos One, 6:22337-, 2011 Cited by PubMed Abstract: P58(IPK) is one of the endoplasmic reticulum- (ER-) localised DnaJ (ERdj) proteins which interact with the chaperone BiP, the mammalian ER ortholog of Hsp70, and are thought to contribute to the specificity and regulation of its diverse functions. P58(IPK), expression of which is upregulated in response to ER stress, has been suggested to act as a co-chaperone, binding un- or misfolded proteins and delivering them to BiP. In order to give further insights into the functions of P58(IPK), and the regulation of BiP by ERdj proteins, we have determined the crystal structure of human P58(IPK) to 3.0 Å resolution using a combination of molecular replacement and single wavelength anomalous diffraction. The structure shows the human P58(IPK) monomer to have a very elongated overall shape. In addition to the conserved J domain, P58(IPK) contains nine N-terminal tetratricopeptide repeat motifs, divided into three subdomains of three motifs each. The J domain is attached to the C-terminal end via a flexible linker, and the structure shows the conserved Hsp70-binding histidine-proline-aspartate (HPD) motif to be situated on the very edge of the elongated protein, 100 Å from the putative binding site for unfolded protein substrates. The residues that comprise the surface surrounding the HPD motif are highly conserved in P58(IPK) from other organisms but more varied between the human ERdj proteins, supporting the view that their regulation of different BiP functions is facilitated by differences in BiP-binding. PubMed: 21799829DOI: 10.1371/JOURNAL.PONE.0022337 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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