2w9r

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{{Seed}}
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==STRUCTURAL BASIS OF N-END RULE SUBSTRATE RECOGNITION IN ESCHERICHIA COLI BY THE CLPAP ADAPTOR PROTEIN CLPS==
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[[Image:2w9r.png|left|200px]]
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<StructureSection load='2w9r' size='340' side='right' caption='[[2w9r]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2w9r]] is a 2 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=2W9R OCA]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[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]]</td></tr>
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<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>
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<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=2w9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w9r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2w9r RCSB], [http://www.ebi.ac.uk/pdbsum/2w9r PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w9/2w9r_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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The line below this paragraph, containing "STRUCTURE_2w9r", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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-->
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{{STRUCTURE_2w9r| PDB=2w9r | SCENE= }}
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===STRUCTURAL BASIS OF N-END RULE SUBSTRATE RECOGNITION IN ESCHERICHIA COLI BY THE CLPAP ADAPTOR PROTEIN CLPS===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<!--
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_19373253}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 19373253 is the PubMed ID number.
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</StructureSection>
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-->
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{{ABSTRACT_PUBMED_19373253}}
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==About this Structure==
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2W9R is a 2 chains structure of sequences 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=2W9R OCA].
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==Reference==
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<ref group="xtra">PMID:19373253</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Albrecht, R.]]
[[Category: Albrecht, R.]]
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[[Category: Clpa]]
[[Category: Clpa]]
[[Category: Clp]]
[[Category: Clp]]
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[[Category: Cytoplasm]]
 
[[Category: Dna condensation]]
[[Category: Dna condensation]]
[[Category: Dna-binding]]
[[Category: Dna-binding]]
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[[Category: N-end rule]]
[[Category: N-end rule]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 6 09:57:40 2009''
 

Revision as of 08:32, 7 May 2014

STRUCTURAL BASIS OF N-END RULE SUBSTRATE RECOGNITION IN ESCHERICHIA COLI BY THE CLPAP ADAPTOR PROTEIN CLPS

2w9r, resolution 1.70Å

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OCA

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