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1ned

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ned FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ned OCA], [http://www.ebi.ac.uk/pdbsum/1ned PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ned RCSB]</span>
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'''CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION'''
'''CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION'''
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[[Category: Groll, M.]]
[[Category: Groll, M.]]
[[Category: Huber, R.]]
[[Category: Huber, R.]]
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[[Category: atp-dependent protease]]
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[[Category: Atp-dependent protease]]
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[[Category: clpq]]
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[[Category: Clpq]]
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[[Category: clpqy]]
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[[Category: Clpqy]]
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[[Category: hslv]]
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[[Category: Hslv]]
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[[Category: hslvu]]
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[[Category: Hslvu]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: proteasome]]
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[[Category: Proteasome]]
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Revision as of 23:26, 2 May 2008

Image:1ned.gif

Template:STRUCTURE 1ned

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 Page seeded by OCA on Sat May 3 02:25:58 2008

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