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2ds5

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(New page: 200px<br /><applet load="2ds5" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ds5, resolution 1.5&Aring;" /> '''Structure of the ZBD ...)
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[[Image:2ds5.gif|left|200px]]<br /><applet load="2ds5" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ds5.gif|left|200px]]<br /><applet load="2ds5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ds5, resolution 1.5&Aring;" />
caption="2ds5, resolution 1.5&Aring;" />
'''Structure of the ZBD in the orthorhomibic crystal from'''<br />
'''Structure of the ZBD in the orthorhomibic crystal from'''<br />
==Overview==
==Overview==
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The degradation of ssrA(AANDENYALAA)-tagged proteins in the bacterial, cytosol is carried out by the ClpXP protease and is markedly stimulated by, the SspB adaptor protein. It has previously been reported that the, amino-terminal zinc-binding domain of ClpX (ZBD) is involved in complex, formation with the SspB-tail (XB: ClpX-binding motif). In an effort to, better understand the recognition of SspB by ClpX and the mechanism of, delivery of ssrA-tagged substrates to ClpXP, we have determined the, structures of ZBD alone at 1.5, 2.0, and 2.5 A resolution in each, different crystal form and also in complex with XB peptide at 1.6 A, resolution. The XB peptide forms an antiparallel beta-sheet with two, beta-strands of ZBD, and the structure shows a 1:1 stoichiometric complex, between ZBD and XB, suggesting that there are two independent, SspB-tail-binding sites in ZBD. The high-resolution ZBD:XB complex, structure, in combination with biochemical analyses, can account for key, determinants in the recognition of the SspB-tail by ClpX and sheds light, on the mechanism of delivery of target proteins to the prokaryotic, degradation machine.
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The degradation of ssrA(AANDENYALAA)-tagged proteins in the bacterial cytosol is carried out by the ClpXP protease and is markedly stimulated by the SspB adaptor protein. It has previously been reported that the amino-terminal zinc-binding domain of ClpX (ZBD) is involved in complex formation with the SspB-tail (XB: ClpX-binding motif). In an effort to better understand the recognition of SspB by ClpX and the mechanism of delivery of ssrA-tagged substrates to ClpXP, we have determined the structures of ZBD alone at 1.5, 2.0, and 2.5 A resolution in each different crystal form and also in complex with XB peptide at 1.6 A resolution. The XB peptide forms an antiparallel beta-sheet with two beta-strands of ZBD, and the structure shows a 1:1 stoichiometric complex between ZBD and XB, suggesting that there are two independent SspB-tail-binding sites in ZBD. The high-resolution ZBD:XB complex structure, in combination with biochemical analyses, can account for key determinants in the recognition of the SspB-tail by ClpX and sheds light on the mechanism of delivery of target proteins to the prokaryotic degradation machine.
==About this Structure==
==About this Structure==
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2DS5 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, CA and PG4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2DS5 OCA].
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2DS5 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>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=PG4:'>PG4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DS5 OCA].
==Reference==
==Reference==
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Structural Basis of SspB-tail Recognition by the Zinc Binding Domain of ClpX., Park EY, Lee BG, Hong SB, Kim HW, Jeon H, Song HK, J Mol Biol. 2007 Mar 23;367(2):514-26. Epub 2007 Jan 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17258768 17258768]
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Structural basis of SspB-tail recognition by the zinc binding domain of ClpX., Park EY, Lee BG, Hong SB, Kim HW, Jeon H, Song HK, J Mol Biol. 2007 Mar 23;367(2):514-26. Epub 2007 Jan 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17258768 17258768]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hong, S.B.]]
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[[Category: Hong, S B.]]
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[[Category: Lee, B.G.]]
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[[Category: Lee, B G.]]
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[[Category: Park, E.Y.]]
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[[Category: Park, E Y.]]
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[[Category: Song, H.K.]]
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[[Category: Song, H K.]]
[[Category: CA]]
[[Category: CA]]
[[Category: PG4]]
[[Category: PG4]]
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[[Category: treble cleft zinc finger]]
[[Category: treble cleft zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:45:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:02:00 2008''

Revision as of 15:02, 21 February 2008


2ds5, resolution 1.5Å

Drag the structure with the mouse to rotate

Structure of the ZBD in the orthorhomibic crystal from

Overview

The degradation of ssrA(AANDENYALAA)-tagged proteins in the bacterial cytosol is carried out by the ClpXP protease and is markedly stimulated by the SspB adaptor protein. It has previously been reported that the amino-terminal zinc-binding domain of ClpX (ZBD) is involved in complex formation with the SspB-tail (XB: ClpX-binding motif). In an effort to better understand the recognition of SspB by ClpX and the mechanism of delivery of ssrA-tagged substrates to ClpXP, we have determined the structures of ZBD alone at 1.5, 2.0, and 2.5 A resolution in each different crystal form and also in complex with XB peptide at 1.6 A resolution. The XB peptide forms an antiparallel beta-sheet with two beta-strands of ZBD, and the structure shows a 1:1 stoichiometric complex between ZBD and XB, suggesting that there are two independent SspB-tail-binding sites in ZBD. The high-resolution ZBD:XB complex structure, in combination with biochemical analyses, can account for key determinants in the recognition of the SspB-tail by ClpX and sheds light on the mechanism of delivery of target proteins to the prokaryotic degradation machine.

About this Structure

2DS5 is a Single protein structure of sequence from Escherichia coli with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis of SspB-tail recognition by the zinc binding domain of ClpX., Park EY, Lee BG, Hong SB, Kim HW, Jeon H, Song HK, J Mol Biol. 2007 Mar 23;367(2):514-26. Epub 2007 Jan 9. PMID:17258768

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