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==STRUCTURAL BASIS OF N-END RULE SUBSTRATE RECOGNITION IN ESCHERICHIA COLI BY THE CLPAP ADAPTOR PROTEIN CLPS - THE PHE PEPTIDE STRUCTURE== | |||
[[Image: | <StructureSection load='2wa8' size='340' side='right' caption='[[2wa8]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2wa8]] is a 4 chain structure with 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=2WA8 OCA]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mbu|1mbu]], [[1lzw|1lzw]], [[2w9r|2w9r]], [[1mg9|1mg9]], [[1mbv|1mbv]], [[1r6o|1r6o]], [[1r6q|1r6q]], [[1mbx|1mbx]], [[2wa9|2wa9]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wa8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wa8 RCSB], [http://www.ebi.ac.uk/pdbsum/2wa8 PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wa/2wa8_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:19373253</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Albrecht, R.]] | [[Category: Albrecht, R.]] | ||
| Line 38: | Line 43: | ||
[[Category: Peptide-binding protein]] | [[Category: Peptide-binding protein]] | ||
[[Category: Phe peptide]] | [[Category: Phe peptide]] | ||
Revision as of 11:37, 7 May 2014
STRUCTURAL BASIS OF N-END RULE SUBSTRATE RECOGNITION IN ESCHERICHIA COLI BY THE CLPAP ADAPTOR PROTEIN CLPS - THE PHE PEPTIDE STRUCTURESTRUCTURAL BASIS OF N-END RULE SUBSTRATE RECOGNITION IN ESCHERICHIA COLI BY THE CLPAP ADAPTOR PROTEIN CLPS - THE PHE PEPTIDE STRUCTURE
Structural highlights
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 PubMedIn 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. References
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