1ned: Difference between revisions

Line 1:

[[Image:1ned.gif|left|200px]]<br /><applet load="1ned" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1ned.gif|left|200px]]<br /><applet load="1ned" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1ned, resolution 3.8Å" />

'''CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION'''<br />

==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.

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 [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1NED OCA].

1NED is a [http://en.wikipedia.org/wiki/Single_protein 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==

Line 25:

[[Category: proteasome]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 22~~:11~~:10 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:11 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1ned.gif|left|200px]]<br /><applet load="1ned" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ned.gif|left|200px]]<br /><applet load="1ned" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ned, resolution 3.8&Aring;" />
 '''CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION'''<br />
 ==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.
+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==
-NED is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NED OCA].
+NED is a [http://en.wikipedia.org/wiki/Single_protein 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==
@@ Line 25: / Line 25: @@
 [[Category: proteasome]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:11:10 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:05:11 2008''