Amino-acid substitutions in a surface turn modulate protein stability.


Abstract

A surface turn position in a four-helix bundle protein, Rop, was selected to investigate the role of turns in protein structure and stability. Although all twenty amino acids can be substituted at this position to generate a correctly folded protein, they produce an unusually large range of thermodynamic stabilities. Moreover, the majority of substitutions give rise to proteins with enhanced thermal stability compared to that of the wild type. By introducing the same twenty mutations at this position, but in a simplified context, we were able to deconvolute intrinsic preferences from local environmental effects. The intrinsic preferences can be explained on the basis of preferred backbone dihedral angles, but local environmental context can significantly modify these effects. Study holds ProTherm entries: 216, 217, 218, 219, 220, 221, 222, 223, 224, 225, 226, 227, 228, 229, 230, 231, 232, 233, 234, 235, 13252, 13253, 13254, 13255, 13256, 13257, 13258, 13259, 13260, 13261, 13262, 13263, 13264, 13265, 13266, 13267, 13268, 13269, 13270 Extra Details: ddG were determined at 69 degrees C (wild type Tm) protein stability; four-helix bundle; Rop; turns;,protein structure; thermodynamic; environmental effects

Submission Details

ID: Mz3eojSu

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:14 p.m.

Version: 1

Publication Details
Predki PF;Agrawal V;BrĂ¼nger AT;Regan L,Nat. Struct. Biol. (1996) Amino-acid substitutions in a surface turn modulate protein stability. PMID:8548455
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
1B6Q 1999-01-16T00:00:00+0000 1.8 ALANINE 31 PROLINE MUTANT OF ROP PROTEIN
1F4M 2000-06-08T00:00:00+0000 2.25 P3(2) CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.
1F4N 2000-06-08T00:00:00+0000 1.9 C2 CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.
1GMG 2001-09-13T00:00:00+0000 1.9 ALANINE 31 PROLINE MUTANT OF ROP PROTEIN, MONOCLINIC FORM
1GTO 1996-04-23T00:00:00+0000 1.82 HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT
1NKD 1997-09-23T00:00:00+0000 1.09 ATOMIC RESOLUTION (1.07 ANGSTROMS) STRUCTURE OF THE ROP MUTANT <2AA>
1QX8 2003-09-04T00:00:00+0000 2.02 Crystal structure of a five-residue deletion mutant of the Rop protein
1ROP 1991-04-02T00:00:00+0000 1.7 STRUCTURE OF THE COL*E1 ROP PROTEIN AT 1.7 ANGSTROMS RESOLUTION
1RPO 1994-08-25T00:00:00+0000 1.4 RESTORED HEPTAD PATTERN CONTINUITY DOES NOT ALTER THE FOLDING OF A 4-ALPHA-HELICAL BUNDLE
1RPR 1991-10-09T00:00:00+0000 0 THE STRUCTURE OF COLE1 ROP IN SOLUTION

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Regulatory protein rop P03051 ROP_ECOLX