6psi

Structural Basis for Client Recognition and Activity of Hsp40 ChaperonesStructural Basis for Client Recognition and Activity of Hsp40 Chaperones

Structural highlights

6psi is a 3 chain structure with sequence from Escherichia coli and Thermus thermophilus HB8. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DNAJ2_THET8 Does not influence ATP binding or hydrolysis nor ADP release. Exerts influence on the interaction of DnaK with substrates; in the presence of DafA, DnaJ inhibits substrate binding, and substrate already bound to DnaK is displaced by DnaJ and DafA.^[1]

References

↑ Klostermeier D, Seidel R, Reinstein J. The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system. J Mol Biol. 1999 Apr 2;287(3):511-25. PMID:10092456 doi:10.1006/jmbi.1999.2636

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OCA

[1] Klostermeier D, Seidel R, Reinstein J. The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system. J Mol Biol. 1999 Apr 2;287(3):511-25. PMID:10092456 doi:10.1006/jmbi.1999.2636

[1]

6psi

Structural Basis for Client Recognition and Activity of Hsp40 ChaperonesStructural Basis for Client Recognition and Activity of Hsp40 Chaperones

Structural highlights

Function

See Also

References

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6psi

Structural Basis for Client Recognition and Activity of Hsp40 ChaperonesStructural Basis for Client Recognition and Activity of Hsp40 Chaperones

Structural highlights

Function

See Also

References

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