PDBsum entry 1ht1

Chaperone

PDB id: 1ht1

Contents

Protein chains

(+ 2 more) 174 a.a. *

408 a.a. *

Ligands

ADP ×4

* Residue conservation analysis

PDB id:

1ht1

Name:

Chaperone

Title:

Nucleotide-dependent conformational changes in a protease-associated atpase hslu

Structure:

Heat shock locus hslv. Chain: c, d, v, x, a, b, z, y. Synonym: atp-dependent protease hslv. Engineered: yes. Heat shock locus hslu. Chain: e, f, g, i. Synonym: atp-dependent hsl protease atp-binding subunit hslu. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 469008. Strain: bl21(de3). Cellular_location: cytoplasm. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Dodecamer (from PDB file)

Resolution:

2.80Å R-factor: 0.261 R-free: 0.309

Authors:

J.Wang,J.J.Song,I.S.Seong,M.C.Franklin,S.Kamtekar,S.H.Eom,C.H.Chung

Key ref:

J.Wang et al. (2001). Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU. Structure, 9, 1107-1116. PubMed id: 11709174 DOI: 10.1016/S0969-2126(01)00670-0

Date:

27-Dec-00 Release date: 14-Nov-01

Protein chains

P0A7B8  (HSLV_ECOLI) -  ATP-dependent protease subunit HslV from Escherichia coli (strain K12)

Seq: 176 a.a.

Struc: 174 a.a.

Protein chains

P0A6H5  (HSLU_ECOLI) -  ATP-dependent protease ATPase subunit HslU from Escherichia coli (strain K12)

Seq: 443 a.a.

Struc: 408 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chains C, D, V, X, A, B, Z, Y: E.C.3.4.25.2 - HslU--HslV peptidase.

DOI no: 10.1016/S0969-2126(01)00670-0

Structure 9:1107-1116 (2001)

PubMed id: 11709174

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

J.Wang, J.J.Song, I.S.Seong, M.C.Franklin, S.Kamtekar, S.H.Eom, C.H.Chung.

ABSTRACT

BACKGROUND: The bacterial heat shock locus ATPase HslU is an AAA(+) protein that has structures known in many nucleotide-free and -bound states. Nucleotide is required for the formation of the biologically active HslU hexameric assembly. The hexameric HslU ATPase binds the dodecameric HslV peptidase and forms an ATP-dependent HslVU protease. RESULTS: We have characterized four distinct HslU conformational states, going sequentially from open to closed: the empty, SO(4), ATP, and ADP states. The nucleotide binds at a cleft formed by an alpha/beta domain and an alpha-helical domain in HslU. The four HslU states differ by a rotation of the alpha-helical domain. This classification leads to a correction of nucleotide identity in one structure and reveals the ATP hydrolysis-dependent structural changes in the HslVU complex, including a ring rotation and a conformational change of the HslU C terminus. This leads to an amended protein unfolding-coupled translocation mechanism. CONCLUSIONS: The observed nucleotide-dependent conformational changes in HslU and their governing principles provide a framework for the mechanistic understanding of other AAA(+) proteins.

Selected figure(s)

Figure 5.
Figure 5. The Binding of ATP-Bound HslU Opens the Central Pore of HslV(a) Uncomplexed HslV has a closed pore [27].(b) The binding of the ATP-bound HslU opens the central pore of HslV with an average diameter of 19.3Å [27]. The HslU C terminus is shown in magenta. The insertion of the C terminus and relative twisting ring rotation may be responsible for the pore opening in a "twist-and-open" mechanism. Two conserved arginines, Arg-86 and Arg-89, are also shown. There are two more positively charged residues, which are not shown, nearby at the pore of HslV (Arg-83 and Lys-90)

The above figure is reprinted by permission from Cell Press: Structure (2001, 9, 1107-1116) copyright 2001.

Figure was selected by an automated process.