Thiol:disulfide interchange protein
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
DsbC active site contains a <scene name='70/705687/Cv/2'>CXXC motif</scene> which modulates the disulfide isomerization and protein folding in the bacterial periplasmic space<ref>PMID:11208797</ref><ref>PMID:11208797</ref>. | DsbC active site contains a <scene name='70/705687/Cv/2'>CXXC motif</scene> which modulates the disulfide isomerization and protein folding in the bacterial periplasmic space<ref>PMID:11208797</ref><ref>PMID:11208797</ref>. | ||
+ | == 3D Structures of thiol:disulfide interchange protein == | ||
+ | [[Thiol:disulfide interchange protein 3D structures]] | ||
+ | |||
</StructureSection> | </StructureSection> | ||
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{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
+ | |||
+ | *Thiol:disulfide interchange protein (DsbA) see [[Protein disulfide oxidoreductase]] | ||
+ | |||
+ | * Thiol:disulfide interchange protein (DsbB) | ||
+ | |||
+ | **[[3e9j], [[2zup]]] – EcDsbB (mutant) + DsbA (mutant) - ''Escherichal coli'' <BR /> | ||
+ | **[[2leg]]] – EcDsbB (mutant) + DsbA (mutant) - NMR<BR /> | ||
+ | **[[2hi7]]] – EcDsbB (mutant) + DsbA (mutant) + ubiquinone <BR /> | ||
+ | **[[2zuq]] – EcDsbB (mutant) + antibody<BR /> | ||
*Thiol:disulfide interchange protein (DsbC) | *Thiol:disulfide interchange protein (DsbC) | ||
- | **[[1eej]], [[1tjd]] – EcDsbC | + | **[[1eej]], [[1tjd]] – EcDsbC <BR /> |
**[[1g0t]], [[1jzo]] – EcDsbC (mutant) <BR /> | **[[1g0t]], [[1jzo]] – EcDsbC (mutant) <BR /> | ||
**[[2iyj]] – EcDsbC N terminal<BR /> | **[[2iyj]] – EcDsbC N terminal<BR /> | ||
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**[[2b1l]], [[2g0f]] – EcDsbE (mutant) <BR /> | **[[2b1l]], [[2g0f]] – EcDsbE (mutant) <BR /> | ||
**[[3kh7]], [[3kh9]] – DsbE soluble domain – ''Pseudomonas aeruginosa''<BR /> | **[[3kh7]], [[3kh9]] – DsbE soluble domain – ''Pseudomonas aeruginosa''<BR /> | ||
+ | |||
+ | *Thiol:disulfide interchange protein (DsbF) | ||
+ | |||
+ | **[[3ios]] – DsbF – ''Mycobacterium tuberculosis'' <BR /> | ||
*Thiol:disulfide interchange protein (DsbG) | *Thiol:disulfide interchange protein (DsbG) |
Revision as of 10:28, 20 February 2020
|
3D Structures of thiol:disulfide interchange protein
Updated on 20-February-2020
{{#tree:id=OrganizedByTopic|openlevels=0|
- Thiol:disulfide interchange protein (DsbA) see Protein disulfide oxidoreductase
- Thiol:disulfide interchange protein (DsbB)
- Thiol:disulfide interchange protein (DsbC)
- Thiol:disulfide interchange protein (DsbD)
- 1l6p, 1jpe, 3pfu, 5nhi – EcDsbD N terminal
- 1uc7, 2fwe, 2fwf 2fwg, 2fwh – EcDsbD C terminal
- 4ip1, 4ip6 – EcDsbD C terminal (mutant)
- 1vrs – EcDsbD N terminal (mutant) + C terminal (mutant)
- 1z5y – EcDsbD N terminal (mutant) + EcDsbE soluble domain (mutant)
- 2k0r, 6dnv, 6dps – NmDsbD N terminal – Neisseria meningitis
- 6dnl, 6dnu – NmDsbD C terminal
- 2k9f – NmDsbD N terminal + thoredoxin
- 1l6p, 1jpe, 3pfu, 5nhi – EcDsbD N terminal
- Thiol:disulfide interchange protein (DsbE)
- Thiol:disulfide interchange protein (DsbF)
- 3ios – DsbF – Mycobacterium tuberculosis
- 3ios – DsbF – Mycobacterium tuberculosis
- Thiol:disulfide interchange protein (DsbG)
- Thiol:disulfide interchange protein (DsbP)
- Thiol:disulfide interchange protein (CycY)
- 1kng – CycY – Bradyrhizobium japonicum
- 1kng – CycY – Bradyrhizobium japonicum
}}
References
- ↑ Rietsch A, Bessette P, Georgiou G, Beckwith J. Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J Bacteriol. 1997 Nov;179(21):6602-8. PMID:9352906
- ↑ Chung J, Chen T, Missiakas D. Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm. Mol Microbiol. 2000 Mar;35(5):1099-109. PMID:10712691
- ↑ Goulding CW, Apostol MI, Gleiter S, Parseghian A, Bardwell J, Gennaro M, Eisenberg D. Gram-positive DsbE proteins function differently from Gram-negative DsbE homologs. A structure to function analysis of DsbE from Mycobacterium tuberculosis. J Biol Chem. 2004 Jan 30;279(5):3516-24. Epub 2003 Nov 3. PMID:14597624 doi:10.1074/jbc.M311833200
- ↑ van Straaten M, Missiakas D, Raina S, Darby NJ. The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli. FEBS Lett. 1998 May 29;428(3):255-8. PMID:9654144
- ↑ Bessette PH, Qiu J, Bardwell JC, Swartz JR, Georgiou G. Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli. J Bacteriol. 2001 Feb;183(3):980-8. PMID:11208797 doi:http://dx.doi.org/10.1128/JB.183.3.980-988.2001
- ↑ Bessette PH, Qiu J, Bardwell JC, Swartz JR, Georgiou G. Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli. J Bacteriol. 2001 Feb;183(3):980-8. PMID:11208797 doi:http://dx.doi.org/10.1128/JB.183.3.980-988.2001
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