Full-length Hsc82 in complex with Aha1 in the presence of AMP-PNPFull-length Hsc82 in complex with Aha1 in the presence of AMP-PNP

Structural highlights

6xlf is a 4 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.15Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HSC82_YEAST Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction such as CNA2. Undergoes a functional cycle that is linked to its ATPase activity (By similarity). Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.[1]

See Also

References

  1. Imai J, Yahara I. Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin. Mol Cell Biol. 2000 Dec;20(24):9262-70. PMID:11094077 doi:10.1128/MCB.20.24.9262-9270.2000

6xlf, resolution 3.15Å

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