Kinetic intermediates in the formation of the cytochrome c molten globule.

Abstract

The relationship between molten globules and transient intermediates in protein folding has been explored by equilibrium and kinetic analysis of the compact acid-denatured A-state of cytochrome c. The chloride-induced formation of the A-state is a complex reaction with structural intermediates resembling those found under native refolding conditions, including a rapidly formed compact state and a subsequent intermediate with interacting N- and C-terminal helices. Together with mutational evidence for specific helix-helix packing interactions, this shows that the A-state is a stable analogue of a late folding intermediate. The L94A mutation blocks all folding steps after the initial collapse and its equilibrium state resembles early kinetic intermediates. Study holds ProTherm entries: 7416, 7417, 7418, 7419, 7420, 7421, 7422, 7423, 14391 Extra Details:

Submission Details

ID: n6Y3Ln2K3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:34 p.m.

Version: 1

Publication Details
Colón W;Roder H,Nat. Struct. Biol. (1996) Kinetic intermediates in the formation of the cytochrome c molten globule. PMID:8946855
Additional Information

Study Summary

Number of data points 18
Proteins Cytochrome c ; Cytochrome c
Unique complexes 3
Assays/Quantities/Protocols Experimental Assay: ddG ; Experimental Assay: Tm ; Experimental Assay: dHvH ; Experimental Assay: Cm ; Experimental Assay: dG_H2O ; Experimental Assay: Cm ; Experimental Assay: dG_H2O ; Derived Quantity: dTm
Libraries Mutations for sequence GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE

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
1KTD 2002-01-15T00:00:00+0000 2.4 CRYSTAL STRUCTURE OF CLASS II MHC MOLECULE IEK BOUND TO PIGEON CYTOCHROME C PEPTIDE
2B4Z 2005-09-27T00:00:00+0000 1.5 Crystal structure of cytochrome C from bovine heart at 1.5 A resolution.
2YBB 2011-03-02T00:00:00+0000 19.0 Fitted model for bovine mitochondrial supercomplex I1III2IV1 by single particle cryo-EM (EMD-1876)
3J2T 2012-12-23T00:00:00+0000 9.5 An improved model of the human apoptosome
5C0Z 2015-06-12T00:00:00+0000 1.12 The structure of oxidized rat cytochrome c at 1.13 angstroms resolution
5C9M 2015-06-28T00:00:00+0000 1.36 The structure of oxidized rat cytochrome c (T28A) at 1.362 angstroms resolution.
5DF5 2015-08-26T00:00:00+0000 1.3 The structure of oxidized rat cytochrome c (T28E) at 1.30 angstroms resolution.
5JUY 2016-05-10T00:00:00+0000 4.1 Active human apoptosome with procaspase-9
6FF5 2018-01-03T00:00:00+0000 1.74 X-ray structure of bovine heart cytochrome c at high ionic strength
6N1O 2018-11-09T00:00:00+0000 1.55 Oxidized rat cytochrome c mutant (S47E)

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Cytochrome c P00004 CYC_HORSE
99.0 Cytochrome c P68097 CYC_EQUAS
99.0 Cytochrome c P68096 CYC_EQUBU
97.1 Cytochrome c P62894 CYC_BOVIN
97.1 Cytochrome c P62895 CYC_PIG
97.1 Cytochrome c P62896 CYC_SHEEP
94.3 Cytochrome c P00007 CYC_HIPAM
95.2 Cytochrome c P68099 CYC_CAMDR
95.2 Cytochrome c P68100 CYC_ESCRO
95.2 Cytochrome c P68098 CYC_LAMGU
94.3 Cytochrome c P62897 CYC_MOUSE
94.3 Cytochrome c P00008 CYC_RABIT
94.3 Cytochrome c P62898 CYC_RAT
94.3 Cytochrome c P00011 CYC_CANLF
93.3 Cytochrome c P00014 CYC_MACGI
93.3 Cytochrome c P00013 CYC_MINSC
93.3 Cytochrome c Q52V09 CYC_CEPBA
93.3 Cytochrome c P00012 CYC_MIRLE
90.5 Cytochrome c Q52V10 CYC_SAISC
92.3 Cytochrome c P81280 CYC_ALLMI
92.2 Cytochrome c P00020 CYC_ANAPL
91.3 Cytochrome c P00021 CYC_COLLI
90.3 Cytochrome c B4USV4 CYC_OTOGA