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==NMR STRUCTURE OF ERP29 C-DOMAIN==
==NMR STRUCTURE OF ERP29 C-DOMAIN==
<StructureSection load='1g7d' size='340' side='right'caption='[[1g7d]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1g7d' size='340' side='right'caption='[[1g7d]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1g7d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G7D FirstGlance]. <br>
<table><tr><td colspan='2'>[[1g7d]] 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=1G7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G7D FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1g7e|1g7e]]</div></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'>[https://proteopedia.org/fgij/fg.htm?mol=1g7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g7d OCA], [https://pdbe.org/1g7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g7d RCSB], [https://www.ebi.ac.uk/pdbsum/1g7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g7d 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=1g7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g7d OCA], [https://pdbe.org/1g7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g7d RCSB], [https://www.ebi.ac.uk/pdbsum/1g7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g7d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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.  
[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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 19: Line 19:
</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=1g7d ConSurf].
</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=1g7d ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: ERp29 is a ubiquitously expressed rat endoplasmic reticulum (ER) protein conserved in mammalian species. Fold predictions suggest the presence of a thioredoxin-like domain homologous to the a domain of human protein disulfide isomerase (PDI) and a helical domain similar to the C-terminal domain of P5-like PDIs. As ERp29 lacks the double-cysteine motif essential for PDI redox activity, it is suggested to play a role in protein maturation and/or secretion related to the chaperone function of PDI. ERp29 self-associates into 51 kDa dimers and also higher oligomers. RESULTS: 3D structures of the N- and C-terminal domains determined by NMR spectroscopy confirmed the thioredoxin fold for the N-terminal domain and yielded a novel all-helical fold for the C-terminal domain. Studies of the full-length protein revealed a short, flexible linker between the two domains, homodimerization by the N-terminal domain, and the presence of interaction sites for the formation of higher molecular weight oligomers. A gadolinium-based relaxation agent is shown to present a sensitive tool for the identification of macromolecular interfaces by NMR. CONCLUSIONS: ERp29 is the first eukaryotic PDI-related protein for which the structures of all domains have been determined. Furthermore, an experimental model of the full-length protein and its association states was established. It is the first example of a protein where the thioredoxin fold was found to act as a specific homodimerization module, without covalent linkages or supporting interactions by further domains. A homodimerization module similar as in ERp29 may also be present in homodimeric human PDI.
Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer.,Liepinsh E, Baryshev M, Sharipo A, Ingelman-Sundberg M, Otting G, Mkrtchian S Structure. 2001 Jun;9(6):457-71. PMID:11435111<ref>PMID:11435111</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1g7d" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[ER-resident protein|ER-resident protein]]
*[[ER-resident protein|ER-resident protein]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Barishev, M]]
[[Category: Rattus norvegicus]]
[[Category: Ingelman-Sundberg, M]]
[[Category: Barishev M]]
[[Category: Liepinsh, E]]
[[Category: Ingelman-Sundberg M]]
[[Category: Mkrtchian, S]]
[[Category: Liepinsh E]]
[[Category: Otting, G]]
[[Category: Mkrtchian S]]
[[Category: Sharipo, A]]
[[Category: Otting G]]
[[Category: Alpha helical protein]]
[[Category: Sharipo A]]
[[Category: Chaperone]]

Revision as of 11:19, 27 March 2024

NMR STRUCTURE OF ERP29 C-DOMAIN

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