2ds6: Difference between revisions

Revision as of 01:33, 28 July 2008

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File:2ds6.png

Template:STRUCTURE 2ds6

Structure of the ZBD in the tetragonal crystal formStructure of the ZBD in the tetragonal crystal form

Template:ABSTRACT PUBMED 17258768

About this StructureAbout this Structure

2DS6 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

Page seeded by OCA on Mon Jul 28 01:33:08 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2ds6.gif|left|200px]]
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 {{STRUCTURE_2ds6|  PDB=2ds6  |  SCENE=  }}
-'''Structure of the ZBD in the tetragonal crystal form'''
+===Structure of the ZBD in the tetragonal crystal form===
-==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.
+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.
+-->
+{{ABSTRACT_PUBMED_17258768}}
 ==About this Structure==
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 [[Category: Substrate binding domain]]
 [[Category: Zinc finger domain]]
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