Protein stability effects of a complete set of alanine substitutions in Arc repressor.
Abstract
The equilibrium stabilities of a complete set of single alanine-substitution mutants of the Arc repressor of bacteriophage P22 have been determined by thermal and urea denaturation experiments. Only half the alanine substitutions cause significant changes in stability, with the most deleterious mutations affecting side chains in the hydrophobic core or in salt bridges and hydrogen bonds which are protected from solvent. The five mutations that are most destabilizing affect a cluster of core residues that seem to form a structural foundation for Arc. Study holds ProTherm entries: 573, 574, 575, 576, 577, 578, 579, 580, 581, 582, 583, 584, 585, 586, 587, 588, 589, 590, 591, 592, 593, 594, 595, 596, 597, 598, 599, 600, 601, 602, 603, 604, 605, 606, 607, 608, 609, 610, 611, 612, 613, 614, 615, 616, 617, 618, 619, 620, 621, 622, 623, 624, 625, 626, 627, 628, 629, 630, 631, 632, 633, 634, 635, 636, 637, 638, 639, 640, 641, 642, 643, 644, 645, 646, 647, 648, 649, 650, 651, 652, 653, 654, 655, 656, 657, 658, 659, 660, 661, 662, 663, 664, 665, 666, 667, 668 Extra Details: additive : EDTA(0.2 mM),Arc st6; carboxy terminal extension with 6 His residues Arc repressor, alanine substitutions; protein stability;,urea denaturation; hydrophobic core; hydrogen bonds
Submission Details
ID: rqShdLt63
Submitter: Connie Wang
Submission Date: April 24, 2018, 8:15 p.m.
Version: 1
Publication Details
Milla ME;Brown BM;Sauer RT,Nat. Struct. Biol. (1994) Protein stability effects of a complete set of alanine substitutions in Arc repressor. PMID:7664079Additional Information
Study Summary
| Number of data points | 286 |
| Proteins | Transcriptional repressor arc ; Transcriptional repressor arc |
| Unique complexes | 47 |
| Assays/Quantities/Protocols | Experimental Assay: Tm ; Experimental Assay: dHvH ; Experimental Assay: m ; Experimental Assay: dG_H2O ; Derived Quantity: dTm ; Derived Quantity: ddG_H2O |
| Libraries | Mutations for sequence MKGMSKMPQFNLRWPREVLDLVRKVAEENGRSVNSEIYQRVMESFKKEGRIGA |
Structure view and single mutant data analysis
Study data
| 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 |
|---|---|---|---|
| 1ARQ | 1994-01-31 | RELAXATION MATRIX REFINEMENT OF THE SOLUTION STRUCTURE OF THE ARC REPRESSOR | |
| 1ARR | 1994-01-31 | RELAXATION MATRIX REFINEMENT OF THE SOLUTION STRUCTURE OF THE ARC REPRESSOR | |
| 1QTG | 1999-07-12 | AVERAGED NMR MODEL OF SWITCH ARC, A DOUBLE MUTANT OF ARC REPRESSOR | |
| 1B28 | 1999-11-03 | ARC REPRESSOR MYL MUTANT FROM SALMONELLA BACTERIOPHAGE P22 | |
| 1NLA | 2003-03-18 | Solution Structure of Switch Arc, a Mutant with 3(10) Helices Replacing a Wild-Type Beta-Ribbon | |
| 1U9P | 2005-02-15 | 1.9 | Permuted single-chain Arc |
| 1BAZ | 1998-06-17 | 1.9 | ARC REPRESSOR MUTANT PHE10VAL |
| 1MYL | 1995-01-26 | 2.4 | SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY |
| 1MYK | 1995-01-26 | 2.4 | CRYSTAL STRUCTURE, FOLDING, AND OPERATOR BINDING OF THE HYPERSTABLE ARC REPRESSOR MUTANT PL8 |
| 1BDT | 1999-02-16 | 2.5 | WILD TYPE GENE-REGULATING PROTEIN ARC/DNA COMPLEX |
| 1PAR | 1994-07-31 | 2.6 | DNA RECOGNITION BY BETA-SHEETS IN THE ARC REPRESSOR-OPERATOR CRYSTAL STRUCTURE |
| 1BDV | 1999-01-06 | 2.8 | ARC FV10 COCRYSTAL |
Relevant UniProtKB Entries
| Percent Identity | Matching Chains | Protein | Accession | Entry Name |
|---|---|---|---|---|
| 100.0 | Transcriptional repressor arc | P03050 | RARC_BPP22 |