Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein.


Abstract

The refolding from denaturing conditions of a small four-helix bundle, the acyl-coenzyme A binding protein, has been investigated by utilizing an array of fast-reaction techniques. Stopped-flow tryptophan fluorescence for measuring the incorporation of aromatic residues into the protein core and far- and near-ultraviolet circular dichroism to measure the formation of secondary and tertiary structure, respectively, together with the formation of persistent structure measured by hydrogen exchange pulse labeling experiments analyzed by electrospray ionisation mass spectrometry all show that 90% of the acyl-coenzyme A binding protein molecules achieve their fully folded and active, native state with a time constant of less than 5 ms at 25 degrees C and of ca. 30 ms at 5 degrees C. The kinetic parameters measured by the different techniques are closely similar, indicating that the different elements of structure form effectively concomitantly. There is no evidence for a significant population of any partially structured intermediate states, and the kinetics are identical whether refolding occurs from an unfolded state generated either by low pH or by addition of guanidine hydrochloride. The kinetics of both refolding and unfolding are monophasic processes for practically 90% of the molecules, and can be described by a two-state model. The results add to our knowledge of the folding scheme of different structural motifs and are discussed in terms of current views of the mechanisms of protein folding. Study holds ProTherm entries: 5092 Extra Details:

Submission Details

ID: jeL2Bvje3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:28 p.m.

Version: 1

Publication Details
Kragelund BB;Robinson CV;Knudsen J;Dobson CM;Poulsen FM,Biochemistry (1995) Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein. PMID:7766632
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
2ABD 1993-07-15 THE THREE-DIMENSIONAL STRUCTURE OF ACYL-COENZYME A BINDING PROTEIN FROM BOVINE LIVER. STRUCTURAL REFINEMENT USING HETERONUCLEAR MULTIDIMENSIONAL NMR SPECTROSCOPY
1ACA 1994-01-31 THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN ACYL-COENZYME A BINDING PROTEIN AND PALMITOYL-COENZYME A
1NVL 2004-05-11 RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Protein, ACBP, in complex with palmitoyl-coenzyme A
1NTI 2004-05-18 RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Protein, ACBP
2CB8 2006-10-25 1.4 High resolution crystal structure of liganded human L-ACBP
2FJ9 2006-10-31 1.6 High resolution crystal structure of the unliganded human ACBP
1HB6 2002-03-11 2.0 Structure of bovine Acyl-CoA binding protein in orthorhombic crystal form
1HB8 2002-03-11 2.0 Structure of bovine Acyl-CoA binding protein in tetragonal crystal form
2FDQ 2006-10-24 3.5 crystal structure of ACBP from Armadillo Harderian Gland

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
92.0 Acyl-CoA-binding protein P12026 ACBP_PIG
93.1 Acyl-CoA-binding protein P07108 ACBP_HUMAN
95.4 Acyl-CoA-binding protein P82934 ACBP_CHAVI
100.0 Acyl-CoA-binding protein P07107 ACBP_BOVIN