1ned: Difference between revisions
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[[Image:1ned.gif|left|200px]] | [[Image:1ned.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION''' | {{Structure | ||
|PDB= 1ned |SIZE=350|CAPTION= <scene name='initialview01'>1ned</scene>, resolution 3.8Å | |||
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'''CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NED is a [ | 1NED is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NED OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9177170 9177170] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: proteasome]] | [[Category: proteasome]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:55:45 2008'' | ||
Revision as of 10:55, 20 March 2008
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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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