1yfn

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[[Image:1yfn.png|left|200px]]
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==Versatile modes of peptide recognition by the AAA+ adaptor protein SspB- the crystal structure of a SspB-RseA complex==
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<StructureSection load='1yfn' size='340' side='right' caption='[[1yfn]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1yfn]] is a 8 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=1YFN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YFN FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ou8|1ou8]], [[1ou9|1ou9]], [[1oul|1oul]], [[1ox8|1ox8]], [[1ox9|1ox9]]</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=1yfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yfn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1yfn RCSB], [http://www.ebi.ac.uk/pdbsum/1yfn 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/yf/1yfn_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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Energy-dependent proteases often rely on adaptor proteins to modulate substrate recognition. The SspB adaptor binds peptide sequences in the stress-response regulator RseA and in ssrA-tagged proteins and delivers these molecules to the AAA+ ClpXP protease for degradation. The structure of SspB bound to an ssrA peptide is known. Here, we report the crystal structure of a complex between SspB and its recognition peptide in RseA. Notably, the RseA sequence is positioned in the peptide-binding groove of SspB in a direction opposite to the ssrA peptide, the two peptides share only one common interaction with the adaptor, and the RseA interaction site is substantially larger than the overlapping ssrA site. This marked diversity in SspB recognition of different target proteins indicates that it is capable of highly flexible and dynamic substrate delivery.
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{{STRUCTURE_1yfn| PDB=1yfn | SCENE= }}
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Versatile modes of peptide recognition by the AAA+ adaptor protein SspB.,Levchenko I, Grant RA, Flynn JM, Sauer RT, Baker TA Nat Struct Mol Biol. 2005 Jun;12(6):520-5. Epub 2005 May 8. PMID:15880122<ref>PMID:15880122</ref>
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===Versatile modes of peptide recognition by the AAA+ adaptor protein SspB- the crystal structure of a SspB-RseA complex===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_15880122}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1yfn]] is a 8 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=1YFN OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:015880122</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Baker, T A.]]
[[Category: Baker, T A.]]

Revision as of 19:13, 29 September 2014

Versatile modes of peptide recognition by the AAA+ adaptor protein SspB- the crystal structure of a SspB-RseA complex

1yfn, resolution 1.80Å

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