2ds6: Difference between revisions
New page: left|200px<br /><applet load="2ds6" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ds6, resolution 2.0Å" /> '''Structure of the ZBD ... |
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[[Image:2ds6.gif|left|200px]]<br /><applet load="2ds6" size=" | [[Image:2ds6.gif|left|200px]]<br /><applet load="2ds6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2ds6, resolution 2.0Å" /> | caption="2ds6, resolution 2.0Å" /> | ||
'''Structure of the ZBD in the tetragonal crystal form'''<br /> | '''Structure of the ZBD in the tetragonal crystal form'''<br /> | ||
==Overview== | ==Overview== | ||
The degradation of ssrA(AANDENYALAA)-tagged proteins in the bacterial | 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== | ||
2DS6 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:// | 2DS6 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=2DS6 OCA]. | ||
==Reference== | ==Reference== | ||
Structural | 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]] | ||
[[Category: Hong, S | [[Category: Hong, S B.]] | ||
[[Category: Lee, B | [[Category: Lee, B G.]] | ||
[[Category: Park, E | [[Category: Park, E Y.]] | ||
[[Category: Song, H | [[Category: Song, H K.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: substrate binding domain]] | [[Category: substrate binding domain]] | ||
[[Category: zinc finger domain]] | [[Category: zinc finger domain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:02:00 2008'' | ||
Revision as of 18:02, 21 February 2008
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Structure of the ZBD in the tetragonal crystal form
OverviewOverview
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 StructureAbout this Structure
2DS6 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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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