(Q27641494)

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Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome

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Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome (English)

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Benedikt M. Kessler

object named as

Benedikt M Kessler

2

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author name string

Ae-Ran Kwon

1

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Herman S Overkleeft

3

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David B McKay

4

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language of work or name

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publication date

4 July 2003

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Journal of Molecular Biology

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330

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2

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185-95

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HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome

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Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli.

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Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY.

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Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli

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Proteolytic activity of the ATP-dependent protease HslVU can be uncoupled from ATP hydrolysis

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The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase

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ATP binding, but not its hydrolysis, is required for assembly and proteolytic activity of the HslVU protease in Escherichia coli

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Crystal structure of heat shock locus V (HslV) from Escherichia coli

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Structure of Haemophilus influenzae HslV protein at 1.9 A resolution, revealing a cation-binding site near the catalytic site

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Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

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Structure of 20S proteasome from yeast at 2.4 A resolution

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Proteasome from Thermoplasma acidophilum: a threonine protease

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The structures of HsIU and the ATP-dependent protease HsIU-HsIV

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Crystal and solution structures of an HslUV protease-chaperone complex

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Structure of Haemophilus influenzae HslU protein in crystals with one-dimensional disorder twinning

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HSP100/Clp proteins: a common mechanism explains diverse functions

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Mutational studies on HslU and its docking mode with HslV

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Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism

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Functional interactions of HslV (ClpQ) with the ATPase HslU (ClpY).

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The C-terminal tails of HslU ATPase act as a molecular switch for activation of HslV peptidase

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Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU

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Crystal structure of HslUV complexed with a vinyl sulfone inhibitor: corroboration of a proposed mechanism of allosteric activation of HslV by HslU

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Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors

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Probing structural determinants distal to the site of hydrolysis that control substrate specificity of the 20S proteasome.

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Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine

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Regulatory role of C-terminal residues of SulA in its degradation by Lon protease in Escherichia coli

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A gated channel into the proteasome core particle

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Structural basis for the activation of 20S proteasomes by 11S regulators

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ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli

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Processing of X-ray diffraction data collected in oscillation mode

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The CCP4 suite: programs for protein crystallography

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The ATP-dependent HslVU/ClpQY protease participates in turnover of cell division inhibitor SulA in Escherichia coli

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10.1016/S0022-2836(03)00580-1

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