1g4a
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CRYSTAL STRUCTURES OF THE HSLVU PEPTIDASE-ATPASE COMPLEX REVEAL AN ATP-DEPENDENT PROTEOLYSIS MECHANISM
OverviewOverview
BACKGROUND: The bacterial heat shock locus HslU ATPase and HslV peptidase, together form an ATP-dependent HslVU protease. Bacterial HslVU is a, homolog of the eukaryotic 26S proteasome. Crystallographic studies of, HslVU should provide an understanding of ATP-dependent protein unfolding, translocation, and proteolysis by this and other ATP-dependent proteases., RESULTS: We present a 3.0 A resolution crystal structure of HslVU with an, HslU hexamer bound at one end of an HslV dodecamer. The structure shows, that the central pores of the ATPase and peptidase are next to each other, and aligned. The central pore of HslU consists of a GYVG motif, which is, conserved among protease-associated ATPases. The binding of one HslU, hexamer to one end of an HslV dodecamer in the 3.0 A resolution structure, opens both HslV central pores and induces asymmetric changes in HslV., CONCLUSIONS: Analysis of nucleotide binding induced conformational changes, in the current and previous HslU structures suggests a protein, unfolding-coupled translocation mechanism. In this mechanism, unfolded, polypeptides are threaded through the aligned pores of the ATPase and, peptidase and translocated into the peptidase central chamber.
About this StructureAbout this Structure
1G4A is a Protein complex structure of sequences from Escherichia coli with DAT as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism., Wang J, Song JJ, Franklin MC, Kamtekar S, Im YJ, Rho SH, Seong IS, Lee CS, Chung CH, Eom SH, Structure. 2001 Feb 7;9(2):177-84. PMID:11250202
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