|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2w9r' size='340' side='right'caption='[[2w9r]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='2w9r' size='340' side='right'caption='[[2w9r]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2w9r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W9R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W9R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2w9r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W9R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W9R FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1lzw|1lzw]], [[1mbu|1mbu]], [[1jre|1jre]], [[1l8h|1l8h]], [[1mg9|1mg9]], [[1mbv|1mbv]], [[1l8i|1l8i]], [[1r6o|1r6o]], [[1jts|1jts]], [[1f33|1f33]], [[1f30|1f30]], [[1r6q|1r6q]], [[1mbx|1mbx]], [[1dps|1dps]]</div></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]] 1.7Å</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=2w9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w9r OCA], [https://pdbe.org/2w9r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w9r RCSB], [https://www.ebi.ac.uk/pdbsum/2w9r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w9r 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=2w9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w9r OCA], [https://pdbe.org/2w9r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w9r RCSB], [https://www.ebi.ac.uk/pdbsum/2w9r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w9r ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CLPS_ECOLI CLPS_ECOLI]] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation. [[https://www.uniprot.org/uniprot/DPS_ECOLI DPS_ECOLI]] During stationary phase, binds the chromosome non-specifically, forming a highly ordered and stable dps-DNA co-crystal within which chromosomal DNA is condensed and protected from diverse damages. It protects DNA from oxidative damage by sequestering intracellular Fe(2+) ion and storing it in the form of Fe(3+) oxyhydroxide mineral, which can be released after reduction. One hydrogen peroxide oxidizes two Fe(2+) ions, which prevents hydroxyl radical production by the Fenton reaction. Dps also protects the cell from UV and gamma irradiation, iron and copper toxicity, thermal stress and acid and base shocks. Also shows a weak catalase activity.<ref>PMID:1340475</ref> <ref>PMID:10403254</ref> <ref>PMID:15205421</ref> <ref>PMID:15534364</ref>
| + | [https://www.uniprot.org/uniprot/CLPS_ECOLI CLPS_ECOLI] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 35: |
Line 35: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Albrecht, R]] | + | [[Category: Albrecht R]] |
| - | [[Category: Dougan, D A]] | + | [[Category: Dougan DA]] |
| - | [[Category: Kralik, S M]] | + | [[Category: Kralik SM]] |
| - | [[Category: Schuenemann, V]] | + | [[Category: Schuenemann V]] |
| - | [[Category: Spall, S K]] | + | [[Category: Spall SK]] |
| - | [[Category: Truscott, K N]] | + | [[Category: Truscott KN]] |
| - | [[Category: Zeth, K]] | + | [[Category: Zeth K]] |
| - | [[Category: Adaptor protein]]
| + | |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Clp]]
| + | |
| - | [[Category: Clpa]]
| + | |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Dna condensation]]
| + | |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Iron]]
| + | |
| - | [[Category: Iron storage]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: N-end rule]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
CLPS_ECOLI Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.
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
In Escherichia coli, the ClpAP protease, together with the adaptor protein ClpS, is responsible for the degradation of proteins bearing an amino-terminal destabilizing amino acid (N-degron). Here, we determined the three-dimensional structures of ClpS in complex with three peptides, each having a different destabilizing residue--Leu, Phe or Trp--at its N terminus. All peptides, regardless of the identity of their N-terminal residue, are bound in a surface pocket on ClpS in a stereo-specific manner. Several highly conserved residues in this binding pocket interact directly with the backbone of the N-degron peptide and hence are crucial for the binding of all N-degrons. By contrast, two hydrophobic residues define the volume of the binding pocket and influence the specificity of ClpS. Taken together, our data suggest that ClpS has been optimized for the binding and delivery of N-degrons containing an N-terminal Phe or Leu.
Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS.,Schuenemann VJ, Kralik SM, Albrecht R, Spall SK, Truscott KN, Dougan DA, Zeth K EMBO Rep. 2009 May;10(5):508-14. Epub 2009 Apr 17. PMID:19373253[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schuenemann VJ, Kralik SM, Albrecht R, Spall SK, Truscott KN, Dougan DA, Zeth K. Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS. EMBO Rep. 2009 May;10(5):508-14. Epub 2009 Apr 17. PMID:19373253 doi:10.1038/embor.2009.62
|
