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2rue

From Proteopedia

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Revision as of 04:56, 25 August 2022

Solution structure of the a' domain of thermophilic fungal protein disulfide (oxidized form, 303K)

Structural highlights

2rue is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2kp1, 2kp2
Activity:	Protein disulfide-isomerase, with EC number 5.3.4.1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PDI_HUMIN] Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer (By similarity).

Publication Abstract from PubMed

Protein disulfide isomerase functions as a folding catalyst in the endoplasmic reticulum. Its b' and a' domains provide substrate-binding sites and undergo a redox-dependent domain rearrangement coupled to an open-closed structural change. Here we determined the first solution structure of the a' domain in its oxidized form and thereby demonstrate that oxidation of the a' domain induces significant conformational changes not only in the vicinity of the active site but also in the distal b'-interfacial segment. Based on these findings, we propose that this conformational transition triggers the domain segregation coupled with the exposure of the hydrophobic surface.

Redox-coupled structural changes of the catalytic a' domain of protein disulfide isomerase.,Inagaki K, Satoh T, Yagi-Utsumi M, Le Gulluche AC, Anzai T, Uekusa Y, Kamiya Y, Kato K FEBS Lett. 2015 Aug 10. pii: S0014-5793(15)00689-4. doi:, 10.1016/j.febslet.2015.07.041. PMID:26272828^[1]

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

References

↑ Inagaki K, Satoh T, Yagi-Utsumi M, Le Gulluche AC, Anzai T, Uekusa Y, Kamiya Y, Kato K. Redox-coupled structural changes of the catalytic a' domain of protein disulfide isomerase. FEBS Lett. 2015 Aug 10. pii: S0014-5793(15)00689-4. doi:, 10.1016/j.febslet.2015.07.041. PMID:26272828 doi:http://dx.doi.org/10.1016/j.febslet.2015.07.041

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rue"

@@ Line 3: / Line 3: @@
 <StructureSection load='2rue' size='340' side='right'caption='[[2rue]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2rue]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_16454 Atcc 16454]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RUE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2rue]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RUE 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;'>[[2kp1|2kp1]], [[2kp2|2kp2]]</div></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></td></tr>
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 16454]]
 [[Category: Large Structures]]
 [[Category: Protein disulfide-isomerase]]

2rue

From Proteopedia

Revision as of 04:56, 25 August 2022

Solution structure of the a' domain of thermophilic fungal protein disulfide (oxidized form, 303K)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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