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| [[Image:2ds6.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2ds6| PDB=2ds6 | SCENE= }} | | {{STRUCTURE_2ds6| PDB=2ds6 | SCENE= }} |
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| '''Structure of the ZBD in the tetragonal crystal form'''
| | ===Structure of the ZBD in the tetragonal crystal form=== |
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| ==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. | | The line below this paragraph, {{ABSTRACT_PUBMED_17258768}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17258768 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17258768}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Substrate binding domain]] | | [[Category: Substrate binding domain]] |
| [[Category: Zinc finger domain]] | | [[Category: Zinc finger domain]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:05:47 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:33:08 2008'' |