5hqp

From Proteopedia

(Difference between revisions)

Revision as of 08:28, 27 May 2020

Crystal structure of the ERp44-peroxiredoxin 4 complex

Structural highlights

5hqp is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2r2j, 3tjg, 3tkp
Gene:	PRDX4 (HUMAN), ERP44, KIAA0573, TXNDC4, UNQ532/PRO1075 (HUMAN)
Activity:	Peroxiredoxin, with EC number 1.11.1.15
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PRDX4_HUMAN] Probably involved in redox regulation of the cell. Regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.^[1] [ERP44_HUMAN] Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1L and ERO1LB in the endoplasmic reticulum.^[2] ^[3]

Publication Abstract from PubMed

ERp44 controls the localization and transport of diverse proteins in the early secretory pathway. The mechanisms that allow client recognition and the source of the oxidative power for forming intermolecular disulfides are as yet unknown. Here we present the structure of ERp44 bound to a client, peroxiredoxin 4. Our data reveal that ERp44 binds the oxidized form of peroxiredoxin 4 via thiol-disulfide interchange reactions. The structure explains the redox-dependent recognition and characterizes the essential non-covalent interactions at the interface. The ERp44-Prx4 covalent complexes can be reduced by glutathione and protein disulfide isomerase family members in the ER, allowing the two components to recycle. This work provides insights into the mechanisms of thiol-mediated protein retention and indicates the key roles of ERp44 in this biochemical cycle to optimize oxidative folding and redox homeostasis.

Crystal Structure of the ERp44-Peroxiredoxin 4 Complex Reveals the Molecular Mechanisms of Thiol-Mediated Protein Retention.,Yang K, Li DF, Wang X, Liang J, Sitia R, Wang CC, Wang X Structure. 2016 Oct 4;24(10):1755-1765. doi: 10.1016/j.str.2016.08.002. Epub 2016, Sep 15. PMID:27642162^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jin DY, Chae HZ, Rhee SG, Jeang KT. Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation. J Biol Chem. 1997 Dec 5;272(49):30952-61. PMID:9388242
↑ Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R. ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J. 2002 Feb 15;21(4):835-44. PMID:11847130 doi:http://dx.doi.org/10.1093/emboj/21.4.835
↑ Anelli T, Alessio M, Bachi A, Bergamelli L, Bertoli G, Camerini S, Mezghrani A, Ruffato E, Simmen T, Sitia R. Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44. EMBO J. 2003 Oct 1;22(19):5015-22. PMID:14517240 doi:http://dx.doi.org/10.1093/emboj/cdg491
↑ Yang K, Li DF, Wang X, Liang J, Sitia R, Wang CC, Wang X. Crystal Structure of the ERp44-Peroxiredoxin 4 Complex Reveals the Molecular Mechanisms of Thiol-Mediated Protein Retention. Structure. 2016 Oct 4;24(10):1755-1765. doi: 10.1016/j.str.2016.08.002. Epub 2016, Sep 15. PMID:27642162 doi:http://dx.doi.org/10.1016/j.str.2016.08.002

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5hqp"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the ERp44-peroxiredoxin 4 complex==
-<StructureSection load='5hqp' size='340' side='right' caption='[[5hqp]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='5hqp' size='340' side='right'caption='[[5hqp]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5hqp]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HQP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HQP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5hqp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HQP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HQP FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2r2j|2r2j]], [[3tjg|3tjg]], [[3tkp|3tkp]]</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRDX4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ERP44, KIAA0573, TXNDC4, UNQ532/PRO1075 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peroxiredoxin Peroxiredoxin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.15 1.11.1.15] </span></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=5hqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hqp OCA], [http://pdbe.org/5hqp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hqp RCSB], [http://www.ebi.ac.uk/pdbsum/5hqp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hqp ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5hqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hqp OCA], [http://pdbe.org/5hqp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hqp RCSB], [http://www.ebi.ac.uk/pdbsum/5hqp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hqp ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 19: / Line 20: @@
 </div>
 <div class="pdbe-citations 5hqp" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[ER-resident protein|ER-resident protein]]
+*[[Peroxiredoxin 3D structures|Peroxiredoxin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Peroxiredoxin]]
 [[Category: Li, D F]]

5hqp

From Proteopedia

Revision as of 08:28, 27 May 2020

Crystal structure of the ERp44-peroxiredoxin 4 complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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