2ds5: Difference between revisions
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[[Image:2ds5.gif|left|200px]] | [[Image:2ds5.gif|left|200px]] | ||
'''Structure of the ZBD in the orthorhomibic crystal from''' | {{Structure | ||
|PDB= 2ds5 |SIZE=350|CAPTION= <scene name='initialview01'>2ds5</scene>, resolution 1.5Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=PG4:TETRAETHYLENE GLYCOL'>PG4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Structure of the ZBD in the orthorhomibic crystal from''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2DS5 is a [ | 2DS5 is a [[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=2DS5 OCA]. | ||
==Reference== | ==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:[http:// | 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://www.ncbi.nlm.nih.gov/pubmed/17258768 17258768] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: treble cleft zinc finger]] | [[Category: treble cleft zinc finger]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:30:50 2008'' |
Revision as of 17:30, 20 March 2008
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, resolution 1.5Å | |||||||
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Ligands: | , and | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structure of the ZBD in the orthorhomibic crystal from
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
2DS5 is a Single protein structure of sequence from Escherichia coli. 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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