Thiol:disulfide interchange protein
From Proteopedia
(Difference between revisions)
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*Thiol:disulfide interchange protein (DsbD) | *Thiol:disulfide interchange protein (DsbD) | ||
| - | **[[1l6p]], [[1jpe]], [[3pfu]] – EcDsbD N terminal<BR /> | + | **[[1l6p]], [[1jpe]], [[3pfu]], [[5nhi]] – EcDsbD N terminal<BR /> |
**[[1uc7]], [[2fwe]], [[2fwf]] [[2fwg]], [[2fwh]] – EcDsbD C terminal<BR /> | **[[1uc7]], [[2fwe]], [[2fwf]] [[2fwg]], [[2fwh]] – EcDsbD C terminal<BR /> | ||
**[[4ip1]], [[4ip6]] – EcDsbD C terminal (mutant)<BR /> | **[[4ip1]], [[4ip6]] – EcDsbD C terminal (mutant)<BR /> | ||
**[[1vrs]] – EcDsbD N terminal (mutant) + C terminal (mutant)<BR /> | **[[1vrs]] – EcDsbD N terminal (mutant) + C terminal (mutant)<BR /> | ||
**[[1z5y]] – EcDsbD N terminal (mutant) + EcDsbE soluble domain (mutant)<BR /> | **[[1z5y]] – EcDsbD N terminal (mutant) + EcDsbE soluble domain (mutant)<BR /> | ||
| - | **[[2k0r]] – NmDsbD N terminal – ''Neisseria meningitis''<BR /> | + | **[[2k0r]], [[6dnv]], [[6dps]] – NmDsbD N terminal – ''Neisseria meningitis''<BR /> |
| + | **[[6dnl]], [[6dnu]] – NmDsbD C terminal <BR /> | ||
**[[2k9f]] – NmDsbD N terminal + thoredoxin<BR /> | **[[2k9f]] – NmDsbD N terminal + thoredoxin<BR /> | ||
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**[[4ml1]], [[4ml6]], [[4mly]] – DsbP – ''Klebsiella pneumoniae'' <BR /> | **[[4ml1]], [[4ml6]], [[4mly]] – DsbP – ''Klebsiella pneumoniae'' <BR /> | ||
| + | |||
| + | *Thiol:disulfide interchange protein (CycY) | ||
| + | |||
| + | **[[1kng]] – CycY – ''Bradyrhizobium japonicum'' <BR /> | ||
}} | }} | ||
Revision as of 18:48, 25 September 2018
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3D Structures of thiol:disulfide interchange protein
Updated on 25-September-2018
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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