1ovx
From Proteopedia
(New page: 200px<br /><applet load="1ovx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ovx" /> '''NMR structure of the E. coli ClpX chaperone ...) |
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| - | [[Image:1ovx.jpg|left|200px]]<br /><applet load="1ovx" size=" | + | [[Image:1ovx.jpg|left|200px]]<br /><applet load="1ovx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ovx" /> | caption="1ovx" /> | ||
'''NMR structure of the E. coli ClpX chaperone zinc binding domain dimer'''<br /> | '''NMR structure of the E. coli ClpX chaperone zinc binding domain dimer'''<br /> | ||
==Overview== | ==Overview== | ||
| - | ClpX (423 amino acids), a member of the Clp/Hsp100 family of molecular | + | ClpX (423 amino acids), a member of the Clp/Hsp100 family of molecular chaperones and the protease, ClpP, comprise a multimeric complex supporting targeted protein degradation in Escherichia coli. The ClpX sequence consists of an NH2-terminal zinc binding domain (ZBD) and a COOH-terminal ATPase domain. Earlier, we have demonstrated that the zinc binding domain forms a constitutive dimer that is essential for the degradation of some ClpX substrates such as gammaO and MuA but is not required for the degradation of other substrates such as green fluorescent protein-SsrA. In this report, we present the NMR solution structure of the zinc binding domain dimer. The monomer fold reveals that ZBD is a member of the treble clef zinc finger family, a motif known to facilitate protein-ligand, protein-DNA, and protein-protein interactions. However, the dimeric ZBD structure is not related to any protein structure in the Protein Data Bank. A trimer-of-dimers model of ZBD is presented, which might reflect the closed state of the ClpX hexamer. |
==About this Structure== | ==About this Structure== | ||
| - | 1OVX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1OVX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OVX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Donaldson, L | + | [[Category: Donaldson, L W.]] |
| - | [[Category: Houry, W | + | [[Category: Houry, W A.]] |
[[Category: Kwan, J.]] | [[Category: Kwan, J.]] | ||
[[Category: Wojtyra, U.]] | [[Category: Wojtyra, U.]] | ||
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[[Category: treble clef zinc finger]] | [[Category: treble clef zinc finger]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:09 2008'' |
Revision as of 12:22, 21 February 2008
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NMR structure of the E. coli ClpX chaperone zinc binding domain dimer
Overview
ClpX (423 amino acids), a member of the Clp/Hsp100 family of molecular chaperones and the protease, ClpP, comprise a multimeric complex supporting targeted protein degradation in Escherichia coli. The ClpX sequence consists of an NH2-terminal zinc binding domain (ZBD) and a COOH-terminal ATPase domain. Earlier, we have demonstrated that the zinc binding domain forms a constitutive dimer that is essential for the degradation of some ClpX substrates such as gammaO and MuA but is not required for the degradation of other substrates such as green fluorescent protein-SsrA. In this report, we present the NMR solution structure of the zinc binding domain dimer. The monomer fold reveals that ZBD is a member of the treble clef zinc finger family, a motif known to facilitate protein-ligand, protein-DNA, and protein-protein interactions. However, the dimeric ZBD structure is not related to any protein structure in the Protein Data Bank. A trimer-of-dimers model of ZBD is presented, which might reflect the closed state of the ClpX hexamer.
About this Structure
1OVX is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of the dimeric zinc binding domain of the chaperone ClpX., Donaldson LW, Wojtyra U, Houry WA, J Biol Chem. 2003 Dec 5;278(49):48991-6. Epub 2003 Oct 1. PMID:14525985
Page seeded by OCA on Thu Feb 21 14:22:09 2008
