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1ned

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{{STRUCTURE_1ned| PDB=1ned | SCENE= }}
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'''CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION'''
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===CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9177170 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9177170}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Proteasome]]
[[Category: Proteasome]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:25:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:19:01 2008''

Revision as of 13:19, 27 July 2008

Image:1ned.png

Template:STRUCTURE 1ned

CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 9177170

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 Sun Jul 27 16:19:01 2008

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