Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase.


Abstract

The reversible denaturation of protein disulfide isomerase proceeds through intermediates that are stabilized by interaction with guanidine hydrochloride. At pH 7.5, the equilibrium denaturation by urea is completely reversible and the transition can be reasonably well-described by a two-state model involving only native and denatured forms. In comparison, the equilibrium denaturation by guanidine hydrochloride occurs in two distinct steps. In the presence of a low constant amount of guanidine hydrochloride (0.5-1.4 M), urea denaturation also becomes biphasic, suggesting the accumulation of an intermediate species that is stabilized by specific interaction with guanidine hydrochloride but not by high concentrations of other salts or other denaturants. Study holds ProTherm entries: 11060, 11061, 11062, 11063, 11064, 11065, 11066, 11067, 11068, 11069, 11070, 11071 Extra Details: additive : EDTA(5 mM),N->I intermediates; two-state model; specific interaction

Submission Details

ID: FG85VKoJ4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:41 p.m.

Version: 1

Publication Details
Morjana NA;McKeone BJ;Gilbert HF,Proc. Natl. Acad. Sci. U.S.A. (1993) Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase. PMID:8460117
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
2BJX 1999-02-09 PROTEIN DISULFIDE ISOMERASE
1MEK 1997-04-21 HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 40 STRUCTURES
1BJX 1999-01-13 HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 STRUCTURES
1X5C 2005-11-15 The solution structure of the second thioredoxin-like domain of human Protein disulfide-isomerase
2K18 2008-04-29 Solution structure of bb' domains of human protein disulfide isomerase
3BJ5 2008-09-30 2.2 Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b' domain
4JU5 2014-02-19 2.28 Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase
3UEM 2011-11-23 2.29 Crystal structure of human PDI bb'a' domains
4EKZ 2013-04-10 2.51 Crystal structure of reduced hPDI (abb'xa')
4EL1 2013-04-10 2.88 Crystal structure of oxidized hPDI (abb'xa')

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
93.5 Protein disulfide-isomerase Q5R5B6 PDIA1_PONAB
93.3 Protein disulfide-isomerase Q2HWU2 PDIA1_MACFU
91.0 Protein disulfide-isomerase P04785 PDIA1_RAT
91.0 Protein disulfide-isomerase P09103 PDIA1_MOUSE
94.1 Protein disulfide-isomerase P07237 PDIA1_HUMAN
91.2 Protein disulfide-isomerase Q8R4U2 PDIA1_CRIGR
100.0 Protein disulfide-isomerase P05307 PDIA1_BOVIN