6o6i

<StructureSection load='6o6i' size='340' side='right'caption='[[6o6i]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>

<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>

</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>

<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>

[[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.

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.

 

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== References ==

[[Category: Buffalo rat]]

[[Category: Bahramzadeh, A]]

[[Category: Huber, T]]

[[Category: Otting, G]]

[[Category: Chaperone]]

[[Category: Pseudocontact shift]]