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2f42

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[[Image:2f42.gif|left|200px]]
 
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{{Structure
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==dimerization and U-box domains of Zebrafish C-terminal of HSP70 interacting protein==
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|PDB= 2f42 |SIZE=350|CAPTION= <scene name='initialview01'>2f42</scene>, resolution 2.50&Aring;
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<StructureSection load='2f42' size='340' side='right'caption='[[2f42]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
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<table><tr><td colspan='2'>[[2f42]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F42 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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|GENE= stub1 (amino acids 112-284) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Danio rerio])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f42 OCA], [https://pdbe.org/2f42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f42 RCSB], [https://www.ebi.ac.uk/pdbsum/2f42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f42 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f42 OCA], [http://www.ebi.ac.uk/pdbsum/2f42 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f42 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/F6NGW2_DANRE F6NGW2_DANRE]
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== Evolutionary Conservation ==
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'''dimerization and U-box domains of Zebrafish C-terminal of HSP70 interacting protein'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f4/2f42_consurf.spt"</scriptWhenChecked>
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The heat-shock proteins Hsp70 and Hsp90 play a crucial role in regulating protein quality control both by refolding and by preventing the aggregation of misfolded proteins. It has recently been shown that Hsp70 and Hsp90 act not only in protein refolding but also cooperate with the C terminus of Hsp70 interacting protein (CHIP), a multidomain ubiquitin ligase, to mediate the degradation of unfolded proteins. We present the crystal structure of the helical linker domain and U-box domain of zebrafish CHIP (DrCHIP-HU). The structure of DrCHIP-HU shows a symmetric homodimer. The conformation of the helical linker domains and the relative positions of the helical and U-box domains differ substantially in DrCHIP-HU from those in a recently published structure of an asymmetric dimer of mammalian (mouse) CHIP. We used an in vitro ubiquitination assay to identify residues, located on two long loops and a central alpha helix of the CHIP U-box domain, that are important for interacting with the ubiquitin-conjugating enzyme UbcH5b. In addition, we used NMR spectroscopy to define a complementary interaction surface located on the N-terminal alpha helix and the L4 and L7 loops of UbcH5b. Our results provide insights into conformational variability in the domain arrangement of CHIP and into U-box-mediated recruitment of UbcH5b for the ubiquitination of Hsp70 and Hsp90 substrates.
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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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==About this Structure==
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</jmolCheckbox>
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2F42 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F42 OCA].
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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/main_output.php?pdb_ID=2f42 ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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Structure and interactions of the helical and U-box domains of CHIP, the C terminus of HSP70 interacting protein., Xu Z, Devlin KI, Ford MG, Nix JC, Qin J, Misra S, Biochemistry. 2006 Apr 18;45(15):4749-59. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16605243 16605243]
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</StructureSection>
[[Category: Danio rerio]]
[[Category: Danio rerio]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Misra, S.]]
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[[Category: Misra S]]
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[[Category: Nix, J C.]]
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[[Category: Nix JC]]
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[[Category: Xu, Z.]]
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[[Category: Xu Z]]
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[[Category: u-box]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:57:39 2008''
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Current revision

dimerization and U-box domains of Zebrafish C-terminal of HSP70 interacting protein

PDB ID 2f42

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