PDBsum entry 1yyf

Chaperone/hydrolase

PDB id: 1yyf

Contents

Protein chains

408 a.a. *

180 a.a. *

Ligands

ADP ×2

* Residue conservation analysis

PDB id:

1yyf

Name:

Chaperone/hydrolase

Title:

Correction of x-ray intensities from an hslv-hslu co-crystal containing lattice translocation defects

Structure:

Atp-dependent hsl protease atp-binding subunit hslu. Chain: a, b. Synonym: heat shock protein hslu. Engineered: yes. Atp-dependent protease hslv. Chain: d, c. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Gene: hslu, htpi. Expressed in: escherichia coli. Expression_system_taxid: 562. Bacillus subtilis. Organism_taxid: 1423. Gene: hslv, clpq, codw. Expression_system_taxid: 562

Biol. unit:

Dodecamer (from PDB file)

Resolution:

4.16Å R-factor: 0.280 R-free: 0.346

Authors:

J.Wang,S.H.Rho,H.H.Park,S.H.Eom

Key ref:

J.Wang et al. (2005). Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects. Acta Crystallogr D Biol Crystallogr, 61, 932-941. PubMed id: 15983416 DOI: 10.1107/S0907444905009546

Date:

24-Feb-05 Release date: 12-Jul-05

Protein chains

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

Seq: 443 a.a.

Struc: 408 a.a.

Protein chains

P39070  (CLPQ_BACSU) -  ATP-dependent protease subunit ClpQ from Bacillus subtilis (strain 168)

Seq: 181 a.a.

Struc: 180 a.a.

Enzyme reactions

• Enzyme class: Chains D, C: E.C.3.4.21.- - ?????

DOI no: 10.1107/S0907444905009546

Acta Crystallogr D Biol Crystallogr 61:932-941 (2005)

PubMed id: 15983416

Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects.

J.Wang, S.H.Rho, H.H.Park, S.H.Eom.

ABSTRACT

Because of lattice-translocation defects, two identical but translated lattices can coexist as a single coherent mosaic block in a crystal. The observed structure in such cases is a weighted sum of two identical but translated structures, one from each lattice; the observed structure factors are a weighted vector sum of the structure factors with identical unit amplitudes but shifted phases. The correction of X-ray intensities from a single crystal containing these defects of the hybrid HslV-HslU complex, which consists of Escherichia coli HslU and Bacillus subtilis HslV (also known as CodW), is reported. When intensities are not corrected, a biologically irrelevant complex (with CodW from one lattice and HslU from another) is implied to exist. Only upon correction does a biologically functional CodW-HslU complex structure emerge.

Selected figure(s)

Figure 1.
Figure 1 Observed alternating sharp-diffuse reflections. In the l direction, strong reflections are observed beyond 4.0 Å (large concentral circles) and some reflections are observed at 3.6 Å (reflections with small circles); in the h and k directions reflections barely pass 4.5 Å. Only the third of the reflections with index l = 3n (boxed) have typical Bragg spots and the remaining reflections have streaky features along the l direction. Data were processed to 4.16 Å, slightly below an ice ring at 4.15 Å.

Figure 6.
Figure 6 Incorrect model containing an extra HslV particle (magenta) at (0, 0, 1/3) fits the uncorrected observed data better than the correct model.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2005, 61, 932-941) copyright 2005.

Figures were selected by an automated process.