3g1b: Difference between revisions
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New page: '''Unreleased structure''' The entry 3g1b is ON HOLD Authors: Roman-Hernandez, G., Grant, R.A., Sauer, R.T., Baker, T.A. Description: THE STRUCTURE OF THE CAULOBACTER CRESCENTUS CLPS P... |
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The | ==The structure of the M53A mutant of Caulobacter crescentus clpS protease adaptor protein in complex with WLFVQRDSKE peptide== | ||
<StructureSection load='3g1b' size='340' side='right'caption='[[3g1b]], [[Resolution|resolution]] 1.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3g1b]] is a 4 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=3G1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G1B FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.448Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3g1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g1b OCA], [https://pdbe.org/3g1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g1b RCSB], [https://www.ebi.ac.uk/pdbsum/3g1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g1b ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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 == | |||
[[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/g1/3g1b_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/main_output.php?pdb_ID=3g1b ConSurf]. | |||
<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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3g1b" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[ATP-dependent Clp protease adaptor protein 3D structures|ATP-dependent Clp protease adaptor protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caulobacter vibrioides]] | |||
[[Category: Large Structures]] | |||
[[Category: Baker TA]] | |||
[[Category: Grant RA]] | |||
[[Category: Roman-Hernandez G]] | |||
[[Category: Sauer RT]] | |||
