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==The structure of the Caulobacter crescentus clpS protease adaptor protein in complex with LLL tripeptide==
==The structure of the Caulobacter crescentus clpS protease adaptor protein in complex with LLL tripeptide==
<StructureSection load='3g19' size='340' side='right' caption='[[3g19]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='3g19' size='340' side='right'caption='[[3g19]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3g19]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cauce Cauce]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G19 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G19 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3g19]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides Caulobacter vibrioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G19 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dnj|3dnj]], [[3g1b|3g1b]]</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]] 1.849&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CC_2467, clpS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=155892 CAUCE])</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=3g19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g19 OCA], [https://pdbe.org/3g19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g19 RCSB], [https://www.ebi.ac.uk/pdbsum/3g19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g19 ProSAT]</span></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=3g19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g19 OCA], [http://pdbe.org/3g19 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g19 RCSB], [http://www.ebi.ac.uk/pdbsum/3g19 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g19 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CLPS_CAUCR CLPS_CAUCR]] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation (By similarity).  
[https://www.uniprot.org/uniprot/CLPS_CAUVC CLPS_CAUVC] Involved in the modulation of the specificity of the ClpAP-mediated ATP-dependent protein degradation.[HAMAP-Rule:MF_00302]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g1/3g19_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g1/3g19_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 20: Line 19:
</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/main_output.php?pdb_ID=3g19 ConSurf].
</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/main_output.php?pdb_ID=3g19 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The N-end rule is a conserved degradation pathway that relates the stability of a protein to its N-terminal amino acid. Here, we present crystal structures of ClpS, the bacterial N-end rule adaptor, alone and engaged with peptides containing N-terminal phenylalanine, leucine, and tryptophan. These structures, together with a previous structure of ClpS bound to an N-terminal tyrosine, illustrate the molecular basis of recognition of the complete set of primary N-end rule amino acids. In each case, the alpha-amino group and side chain of the N-terminal residue are the major determinants of recognition. The binding pocket for the N-end residue is preformed in the free adaptor, and only small adjustments are needed to accommodate N-end rule residues having substantially different sizes and shapes. M53A ClpS is known to mediate degradation of an expanded repertoire of substrates, including those with N-terminal valine or isoleucine. A structure of Met53A ClpS engaged with an N-end rule tryptophan reveals an essentially wild-type mechanism of recognition, indicating that the Met(53) side chain directly enforces specificity by clashing with and excluding beta-branched side chains. Finally, experimental and structural data suggest mechanisms that make proteins with N-terminal methionine bind very poorly to ClpS, explaining why these high-abundance proteins are not degraded via the N-end rule pathway in the cell.


Molecular basis of substrate selection by the N-end rule adaptor protein ClpS.,Roman-Hernandez G, Grant RA, Sauer RT, Baker TA Proc Natl Acad Sci U S A. 2009 Jun 2;106(22):8888-93. Epub 2009 May 18. PMID:19451643<ref>PMID:19451643</ref>
==See Also==
 
*[[ATP-dependent Clp protease adaptor protein 3D structures|ATP-dependent Clp protease adaptor protein 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3g19" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cauce]]
[[Category: Caulobacter vibrioides]]
[[Category: Baker, T A]]
[[Category: Large Structures]]
[[Category: Grant, R A]]
[[Category: Baker TA]]
[[Category: Roman-Hernandez, G]]
[[Category: Grant RA]]
[[Category: Sauer, R T]]
[[Category: Roman-Hernandez G]]
[[Category: Adaptor]]
[[Category: Sauer RT]]
[[Category: Peptide binding protein]]
[[Category: Peptide-binding protein]]
[[Category: Protein-peptide complex]]
Retrieved from "https://proteopedia.org/3g19"