6xlh

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Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaSAsymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS

Structural highlights

6xlh 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 2.83Å
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

6xlh, resolution 2.83Å

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