1ned

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spinqualitylabelsall models 1ned, resolution 3.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION

Overview

Heat shock locus V (HslV; also called ClpQ) is the proteolytic core of the, ATP-dependent protease HslVU in Escherichia coli. It has sequence, similarity with the beta-type subunits of the eukaryotic and, archaebacterial proteasomes. Unlike these particles, which display, 72-point symmetry, it is a dimer of hexamers with 62-point symmetry. The, crystal structure of HslV at 3.8-A resolution, determined by isomorphous, replacement and symmetry averaging, shows that in spite of the different, symmetry of the particle, the fold and the contacts between subunits are, conserved. A tripeptide aldehyde inhibitor, acetyl-Leu-Leu-norleucinal, binds to the N-terminal threonine residue of HslV, probably as a, hemiacetal, relating HslV also functionally to the proteasomes of archaea, and eukaryotes.

About this Structure

1NED is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of heat shock locus V (HslV) from Escherichia coli., Bochtler M, Ditzel L, Groll M, Huber R, Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6070-4. PMID:9177170

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