The Crystal Structure of the Human Co-Chaperone P58IPK
Publication Date
July 25, 2011
Journal
PLOS ONE
Authors
Maria Svärd, Ekaterina I. Biterova, Jean Marie Bourhis & Jodie E. Guy
Volume
6
Issue
7
Pages
e22337
DOI
https://dx.plos.org/10.1371/journal.pone.0022337
Publisher URL
http://journals.plos.org/plosone/article?id=10.1371%2Fjournal.pone.0022337
PubMed
http://www.ncbi.nlm.nih.gov/pubmed/21799829
PubMed Central
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3143134
Europe PMC
http://europepmc.org/abstract/MED/21799829
Web of Science
000293172900023
Scopus
79960731117
Mendeley
http://www.mendeley.com/research/crystal-structure-human-cochaperone-p58-ipk
Events
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Mendeley | Further Information

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Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/753115"], "description"=>"<p>Data in parentheses are for the highest resolution shell.</p>", "links"=>[], "tags"=>["biophysics", "Biochemistry"], "article_id"=>423486, "categories"=>["Biochemistry", "Biophysics"], "users"=>["Maria Svärd", "Ekaterina I. Biterova", "Jean-Marie Bourhis", "Jodie E. Guy"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0022337.t001", "stats"=>{"downloads"=>2, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Data_collection_statistics_/423486", "title"=>"Data collection statistics.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2011-07-25 00:58:06"}
  • {"files"=>["https://ndownloader.figshare.com/files/752707"], "description"=>"<p>(A) A cartoon representation of the structure of human P58<sup>IPK</sup>, coloured from blue at the N-terminus to red at the C-terminus. (B) A surface representation of P58<sup>IPK</sup>, with the three TPR subdomains and the J domain depicted in blue, green, yellow and red, respectively.</p>", "links"=>[], "tags"=>["biophysics", "Biochemistry"], "article_id"=>423081, "categories"=>["Biochemistry", "Biophysics"], "users"=>["Maria Svärd", "Ekaterina I. Biterova", "Jean-Marie Bourhis", "Jodie E. Guy"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0022337.g001", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Overall_structure_of_human_P58_IPK_/423081", "title"=>"Overall structure of human P58<sup>IPK</sup>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-25 00:51:21"}
  • {"files"=>["https://ndownloader.figshare.com/files/753091"], "description"=>"<p>Refinement and model building statistics.</p>", "links"=>[], "tags"=>["biophysics", "Biochemistry"], "article_id"=>423464, "categories"=>["Biochemistry", "Biophysics"], "users"=>["Maria Svärd", "Ekaterina I. Biterova", "Jean-Marie Bourhis", "Jodie E. Guy"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0022337.t002", "stats"=>{"downloads"=>1, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Refinement_and_model_building_statistics_/423464", "title"=>"Refinement and model building statistics.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2011-07-25 00:57:44"}
  • {"files"=>["https://ndownloader.figshare.com/files/378924"], "description"=>"<div><p>P58<sup>IPK</sup> is one of the endoplasmic reticulum- (ER-) localised DnaJ (ERdj) proteins which interact with the chaperone BiP, the mammalian ER ortholog of Hsp70, and are thought to contribute to the specificity and regulation of its diverse functions. P58<sup>IPK</sup>, expression of which is upregulated in response to ER stress, has been suggested to act as a co-chaperone, binding un- or misfolded proteins and delivering them to BiP. In order to give further insights into the functions of P58<sup>IPK</sup>, and the regulation of BiP by ERdj proteins, we have determined the crystal structure of human P58<sup>IPK</sup> to 3.0 Å resolution using a combination of molecular replacement and single wavelength anomalous diffraction. The structure shows the human P58<sup>IPK</sup> monomer to have a very elongated overall shape. In addition to the conserved J domain, P58<sup>IPK</sup> contains nine N-terminal tetratricopeptide repeat motifs, divided into three subdomains of three motifs each. The J domain is attached to the C-terminal end via a flexible linker, and the structure shows the conserved Hsp70-binding histidine-proline-aspartate (HPD) motif to be situated on the very edge of the elongated protein, 100 Å from the putative binding site for unfolded protein substrates. The residues that comprise the surface surrounding the HPD motif are highly conserved in P58<sup>IPK</sup> from other organisms but more varied between the human ERdj proteins, supporting the view that their regulation of different BiP functions is facilitated by differences in BiP-binding.</p> </div>", "links"=>[], "tags"=>["co-chaperone"], "article_id"=>134886, "categories"=>["Biochemistry", "Biophysics"], "users"=>["Maria Svärd", "Ekaterina I. Biterova", "Jean-Marie Bourhis", "Jodie E. Guy"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0022337", "stats"=>{"downloads"=>0, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/The_Crystal_Structure_of_the_Human_Co_Chaperone_P58_IPK_/134886", "title"=>"The Crystal Structure of the Human Co-Chaperone P58<sup>IPK</sup>", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-25 01:21:26"}
  • {"files"=>["https://ndownloader.figshare.com/files/752919"], "description"=>"<p>(A) Alignment of sequences of the J domains from the human ERdj proteins. The surface residues mentioned in the text are labelled, using (*) for the residues of the conserved HPD motif, (#) for residues of the adjacent hydrophobic patch in human P58<sup>IPK</sup>, and (§) for positively charged residues on helix II. Conserved residues are shown with red background, and residue numbering corresponds to human P58<sup>IPK</sup>. (B) Sequence alignment of the J domains from P58<sup>IPK</sup> from different species. Labelling is the same as in (A).</p>", "links"=>[], "tags"=>["domains", "erdj", "proteins"], "article_id"=>423293, "categories"=>["Biochemistry", "Biophysics"], "users"=>["Maria Svärd", "Ekaterina I. Biterova", "Jean-Marie Bourhis", "Jodie E. Guy"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0022337.g004", "stats"=>{"downloads"=>0, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Sequence_conservation_between_J_domains_from_the_human_ERdj_proteins_and_from_P58_IPK_from_different_species_/423293", "title"=>"Sequence conservation between J domains from the human ERdj proteins and from P58<sup>IPK</sup> from different species.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-25 00:54:53"}
  • {"files"=>["https://ndownloader.figshare.com/files/752787"], "description"=>"<p>A superimposition of the human P58<sup>IPK</sup> structure and the previously published structure of the TPR domain of mouse P58<sup>IPK</sup>. Human P58<sup>IPK</sup> is coloured from blue at the N-terminus to red at the C-terminus, the TPR domain of mouse P58<sup>IPK</sup> in grey. The structural alignment was based on TPR subdomain II.</p>", "links"=>[], "tags"=>["tpr"], "article_id"=>423158, "categories"=>["Biochemistry", "Biophysics"], "users"=>["Maria Svärd", "Ekaterina I. Biterova", "Jean-Marie Bourhis", "Jodie E. Guy"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0022337.g002", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Comparison_between_human_and_mouse_P58_IPK_TPR_domains_/423158", "title"=>"Comparison between human and mouse P58<sup>IPK</sup> TPR domains.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-25 00:52:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/752848"], "description"=>"<p>(A) A cartoon representation of the J domain of P58<sup>IPK</sup>. The residues of the HPD motif are shown in stick representation and coloured by atom type with carbon in grey, oxygen in red, and nitrogen in blue. (B) A surface representation of the J domain, showing the electrostatic surface potential with positively charged regions in blue and negatively charged regions in red. Positively charged residues on helix II are labelled. (C) A surface representation of the J domain, with hydrophobic residues in green. Residues contributing to the hydrophobic patch adjacent to the HPD motif are labelled.</p>", "links"=>[], "tags"=>["biophysics", "Biochemistry"], "article_id"=>423219, "categories"=>["Biochemistry", "Biophysics"], "users"=>["Maria Svärd", "Ekaterina I. Biterova", "Jean-Marie Bourhis", "Jodie E. Guy"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0022337.g003", "stats"=>{"downloads"=>1, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_J_domain_of_P58_IPK_/423219", "title"=>"The J domain of P58<sup>IPK</sup>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-25 00:53:39"}
  • {"files"=>["https://ndownloader.figshare.com/files/753021"], "description"=>"<p>(A) Surface representations of human P58<sup>IPK</sup>, with hydrophobic residues highlighted in green. (B) Electrostatic surface representations with positively charged regions in blue and negatively charged regions in red.</p>", "links"=>[], "tags"=>["biophysics", "Biochemistry"], "article_id"=>423396, "categories"=>["Biochemistry", "Biophysics"], "users"=>["Maria Svärd", "Ekaterina I. Biterova", "Jean-Marie Bourhis", "Jodie E. Guy"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0022337.g005", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_surface_of_P58_IPK_/423396", "title"=>"The surface of P58<sup>IPK</sup>.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2011-07-25 00:56:36"}

PMC Usage Stats | Further Information

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  • {"unique-ip"=>"5", "full-text"=>"6", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"7"}
  • {"unique-ip"=>"7", "full-text"=>"7", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"3"}
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  • {"unique-ip"=>"3", "full-text"=>"3", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2015", "month"=>"10"}
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  • {"unique-ip"=>"5", "full-text"=>"4", "pdf"=>"3", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2014", "month"=>"9"}
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Relative Metric

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