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
1RPR 1994-01-31 THE STRUCTURE OF COLE1 ROP IN SOLUTION
1NKD 1999-03-23 1.09 ATOMIC RESOLUTION (1.07 ANGSTROMS) STRUCTURE OF THE ROP MUTANT <2AA>
4DO2 2013-02-13 1.4 Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.
1RPO 1995-02-14 1.4 RESTORED HEPTAD PATTERN CONTINUITY DOES NOT ALTER THE FOLDING OF A 4-ALPHA-HELICAL BUNDLE
2IJK 2007-10-16 1.55 Structure of a Rom protein dimer at 1.55 angstrom resolution
1ROP 1992-07-15 1.7 STRUCTURE OF THE COL*E1 ROP PROTEIN AT 1.7 ANGSTROMS RESOLUTION
2IJH 2007-10-16 1.8 Crystal structure analysis of ColE1 ROM mutant F14W
1B6Q 1999-07-09 1.8 ALANINE 31 PROLINE MUTANT OF ROP PROTEIN
1GTO 1997-01-27 1.82 HIGH RESOLUTION STRUCTURE OF A HYPERSTABLE HELICAL BUNDLE PROTEIN MUTANT
2IJJ 2007-10-16 1.9 Crystal structure analysis of ColE1 ROM mutant F14Y
1GMG 2002-09-12 1.9 ALANINE 31 PROLINE MUTANT OF ROP PROTEIN, MONOCLINIC FORM
1F4N 2001-01-10 1.9 C2 CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.
3K79 2010-02-02 1.96 C38A, C52V Cysteine-Free Variant of Rop (Rom)
1QX8 2004-09-28 2.02 Crystal structure of a five-residue deletion mutant of the Rop protein
1F4M 2001-01-10 2.25 P3(2) CRYSTAL STRUCTURE OF ALA2ILE2-6, A VERSION OF ROP WITH A REPACKED HYDROPHOBIC CORE AND A NEW FOLD.
2IJI 2007-10-16 2.3 Structure of F14H mutant of ColE1 Rom protein
2GHY 2006-05-30 2.5 Novel Crystal Form of the ColE1 Rom Protein
1YO7 2005-02-15 2.8 Re-engineering topology of the homodimeric ROP protein into a single-chain 4-helix bundle

Relevant UniProtKB Entries

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