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==Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: Structure Determination from Backbone Amide Pseudocontact Shifts Generated by Double-histidine Cobalt Tags==
==Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: Structure Determination from Backbone Amide Pseudocontact Shifts Generated by Double-histidine Cobalt Tags==
<StructureSection load='6o6i' size='340' side='right'caption='[[6o6i]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='6o6i' size='340' side='right'caption='[[6o6i]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6o6i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O6I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O6I FirstGlance]. <br>
<table><tr><td colspan='2'>[[6o6i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O6I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O6I FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Erp29 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=6o6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o6i OCA], [http://pdbe.org/6o6i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o6i RCSB], [http://www.ebi.ac.uk/pdbsum/6o6i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o6i ProSAT]</span></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=6o6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o6i OCA], [https://pdbe.org/6o6i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o6i RCSB], [https://www.ebi.ac.uk/pdbsum/6o6i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o6i ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ERP29_RAT ERP29_RAT]] Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER.
[https://www.uniprot.org/uniprot/ERP29_RAT ERP29_RAT] Does not seem to be a disulfide isomerase. Plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pseudocontact shifts (PCSs) generated by paramagnetic metal ions contribute highly informative long-range structure restraints that can be measured in solution and are ideally suited to guide structure prediction algorithms in determining global protein folds. We recently demonstrated that PCSs, which are relatively small but of high quality, can be generated by a double-histidine (dHis) motif in an alpha-helix, which provides a well-defined binding site for a single Co(2+) ion. Here we show that PCSs of backbone amide protons generated by dHis-Co(2+) motifs positioned in four different alpha-helices of a protein deliver excellent restraints to determine the three-dimensional (3D) structure of a protein in a way akin to the global positioning system (GPS). We demonstrate the approach with GPS-Rosetta calculations of the 3D structure of the C-terminal domain of the chaperone ERp29 (ERp29-C). Despite the relatively small size of the PCSs generated by the dHis-Co(2+) motifs, the structure calculations converged readily. Generating PCSs by the dHis-Co(2+) motif thus presents an excellent alternative to the use of lanthanide tags.


Three-Dimensional Protein Structure Determination Using Pseudocontact Shifts of Backbone Amide Protons Generated by Double-Histidine Co(2+)-Binding Motifs at Multiple Sites.,Bahramzadeh A, Huber T, Otting G Biochemistry. 2019 Jul 19. doi: 10.1021/acs.biochem.9b00404. PMID:31282649<ref>PMID:31282649</ref>
==See Also==
 
*[[ER-resident protein|ER-resident protein]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6o6i" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bahramzadeh, A]]
[[Category: Rattus norvegicus]]
[[Category: Huber, T]]
[[Category: Bahramzadeh A]]
[[Category: Otting, G]]
[[Category: Huber T]]
[[Category: Chaperone]]
[[Category: Otting G]]
[[Category: Dhis-co2+]]
[[Category: Gps-rosetta structure]]
[[Category: Pseudocontact shift]]

Latest revision as of 07:36, 1 May 2024

Endoplasmic reticulum protein 29 (ERp29) C-terminal domain: Structure Determination from Backbone Amide Pseudocontact Shifts Generated by Double-histidine Cobalt Tags

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