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1YYF

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

Summary for 1YYF
Entry DOI10.2210/pdb1yyf/pdb
DescriptorATP-dependent hsl protease ATP-binding subunit hslU, ATP-dependent protease hslV, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
Functional Keywordslattice translocation defect, hslv-hslu, atp-dependent proteolysis, quaternary structure, chaperone-hydrolase complex, chaperone/hydrolase
Biological sourceEscherichia coli
More
Cellular locationCytoplasm: P0A6H5
Cytoplasm (By similarity): P39070
Total number of polymer chains4
Total formula weight139180.47
Authors
Wang, J.,Rho, S.H.,Park, H.H.,Eom, S.H. (deposition date: 2005-02-24, release date: 2005-07-12, Last modification date: 2024-02-14)
Primary citationWang, J.,Rho, S.H.,Park, H.H.,Eom, S.H.
Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects.
Acta Crystallogr.,Sect.D, 61:932-941, 2005
Cited by
PubMed 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.
PubMed: 15983416
DOI: 10.1107/S0907444905009546
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.16 Å)
Structure validation

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