The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP.


Abstract

The acyl-coenzyme A-binding proteins (ACBPs) contain 26 highly conserved sequence positions. The majority of these have been mutated in the bovine protein, and their influence on the rate of two-state folding and unfolding has been measured. The results identify eight sequence positions, out of 24 probed, that are critical for fast productive folding. The residues are all hydrophobic and located in the interface between the N- and C-terminal helices. The results suggest that one specific site dominated by conserved hydrophobic residues forms the structure of the productive rate-determining folding step and that a sequential framework model can describe the protein folding reaction. Study holds ProTherm entries: 6983, 6984, 6985, 6986, 6987, 6988, 6989, 6990, 6991, 6992, 6993, 6994, 6995, 6996, 6997, 6998, 6999, 7000, 7001, 7002, 7003, 7004, 7005, 7006, 7007, 7008, 7009, 7010, 7011, 7012, 7013 Extra Details: two-state folding; hydrophobic; rate-determining folding step;,sequential framework model; protein folding

Submission Details

ID: DoDZt8HY3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:32 p.m.

Version: 1

Publication Details
Kragelund BB;Osmark P;Neergaard TB;SchiĆødt J;Kristiansen K;Knudsen J;Poulsen FM,Nat. Struct. Biol. (1999) The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP. PMID:10360367
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
2FDQ 2005-12-14T00:00:00+0000 3.5 crystal structure of ACBP from Armadillo Harderian Gland
2CB8 2006-01-03T00:00:00+0000 1.4 High resolution crystal structure of liganded human L-ACBP
2FJ9 2006-01-02T00:00:00+0000 1.6 High resolution crystal structure of the unliganded human ACBP
1ACA 1992-11-17T00:00:00+0000 0 THREE-DIMENSIONAL STRUCTURE OF THE COMPLEX BETWEEN ACYL-COENZYME A BINDING PROTEIN AND PALMITOYL-COENZYME A
1HB6 2001-04-12T00:00:00+0000 2.0 Structure of bovine Acyl-CoA binding protein in orthorhombic crystal form
1HB8 2001-04-12T00:00:00+0000 2.0 Structure of bovine Acyl-CoA binding protein in tetragonal crystal form
1NTI 2003-01-30T00:00:00+0000 0 RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Protein, ACBP
1NVL 2003-02-04T00:00:00+0000 0 RDC-refined NMR structure of bovine Acyl-coenzyme A Binding Protein, ACBP, in complex with palmitoyl-coenzyme A
2ABD 1993-03-05T00:00:00+0000 0 THE THREE-DIMENSIONAL STRUCTURE OF ACYL-COENZYME A BINDING PROTEIN FROM BOVINE LIVER. STRUCTURAL REFINEMENT USING HETERONUCLEAR MULTIDIMENSIONAL NMR SPECTROSCOPY

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