2qwo

File:2qwo.jpg

spinqualitylabelsall models PDB ID 2qwo Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 1.700Å
Ligands:	, , , , and
Gene:	HSPA8, HSC70 (Bos taurus), DNAJC6 (Bos taurus)
Activity:	Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Coordinates:	save as pdb, mmCIF, xml

Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)R171C and bovine Auxilin (810-910aa)D876C in the ADP*Pi form #1

OverviewOverview

The many protein processing reactions of the ATP-hydrolyzing Hsp70s are regulated by J cochaperones, which contain J domains that stimulate Hsp70 ATPase activity and accessory domains that present protein substrates to Hsp70s. We report the structure of a J domain complexed with a J responsive portion of a mammalian Hsp70. The J domain activates ATPase activity by directing the linker that connects the Hsp70 nucleotide binding domain (NBD) and substrate binding domain (SBD) toward a hydrophobic patch on the NBD surface. Binding of the J domain to Hsp70 displaces the SBD from the NBD, which may allow the SBD flexibility to capture diverse substrates. Unlike prokaryotic Hsp70, the SBD and NBD of the mammalian chaperone interact in the ADP state. Thus, although both nucleotides and J cochaperones modulate Hsp70 NBD:linker and NBD:SBD interactions, the intrinsic persistence of those interactions differs in different Hsp70s and this may optimize their activities for different cellular roles.

About this StructureAbout this Structure

2QWO is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of J cochaperone binding and regulation of Hsp70., Jiang J, Maes EG, Taylor AB, Wang L, Hinck AP, Lafer EM, Sousa R, Mol Cell. 2007 Nov 9;28(3):422-33. PMID:17996706

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