|
|
| (2 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Structure of the ZBD-XB complex== | | ==Structure of the ZBD-XB complex== |
| - | <StructureSection load='2ds8' size='340' side='right' caption='[[2ds8]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='2ds8' size='340' side='right'caption='[[2ds8]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ds8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DS8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DS8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ds8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DS8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ds5|2ds5]], [[2ds6|2ds6]], [[2ds7|2ds7]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ds8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ds8 OCA], [http://pdbe.org/2ds8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ds8 RCSB], [http://www.ebi.ac.uk/pdbsum/2ds8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ds8 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ds8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ds8 OCA], [https://pdbe.org/2ds8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ds8 RCSB], [https://www.ebi.ac.uk/pdbsum/2ds8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ds8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CLPX_ECOLI CLPX_ECOLI]] ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized and readily hydrolyzed by ClpP. Can perform chaperone functions in the absence of ClpP.[HAMAP-Rule:MF_00175] | + | [https://www.uniprot.org/uniprot/CLPX_ECOLI CLPX_ECOLI] ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized and readily hydrolyzed by ClpP. Can perform chaperone functions in the absence of ClpP.[HAMAP-Rule:MF_00175] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 29: |
Line 29: |
| | </div> | | </div> |
| | <div class="pdbe-citations 2ds8" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2ds8" style="background-color:#fffaf0;"></div> |
| - | | |
| - | ==See Also== | |
| - | *[[ClpX|ClpX]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Hong, S B]] | + | [[Category: Large Structures]] |
| - | [[Category: Kim, H W]] | + | [[Category: Hong SB]] |
| - | [[Category: Lee, B G]] | + | [[Category: Kim HW]] |
| - | [[Category: Park, E Y]] | + | [[Category: Lee BG]] |
| - | [[Category: Song, H K]] | + | [[Category: Park EY]] |
| - | [[Category: Metal binding protein]] | + | [[Category: Song HK]] |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Protein-peptide complex]]
| + | |
| Structural highlights
Function
CLPX_ECOLI ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized and readily hydrolyzed by ClpP. Can perform chaperone functions in the absence of ClpP.[HAMAP-Rule:MF_00175]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Park EY, Lee BG, Hong SB, Kim HW, Jeon H, Song HK. Structural basis of SspB-tail recognition by the zinc binding domain of ClpX. J Mol Biol. 2007 Mar 23;367(2):514-26. Epub 2007 Jan 9. PMID:17258768 doi:10.1016/j.jmb.2007.01.003
|
