1MYL

SUBSTITUTING HYDROPHOBIC RESIDUES FOR A BURIED SALT BRIDGE ENHANCES PROTEIN STABILITY BUT DOES NOT REDUCE CONFORMATIONAL SPECIFICITY

Summary for 1MYL

• Entry DOI: 10.2210/pdb1myl/pdb
• Descriptor: ARC REPRESSOR (2 entities in total)
• Functional Keywords: transcription regulation, hyperstable mutant
• Biological source: Enterobacteria phage P22
• Total number of polymer chains: 6
• Total formula weight: 37213.79

Authors

Schildbach, J.F.,Waldburger, C.D.,Sauer, R.T. (deposition date: 1994-10-06, release date: 1995-01-26, Last modification date: 2024-02-14)

Primary citation

Waldburger, C.D.,Schildbach, J.F.,Sauer, R.T.
Are buried salt bridges important for protein stability and conformational specificity?
Nat.Struct.Biol., 2:122-128, 1995

PubMed Abstract: The side chains of Arg 31, Glu 36 and Arg 40 in Arc repressor form a buried salt-bridge triad. The entire salt-bridge network can be replaced by hydrophobic residues in combinatorial randomization experiments resulting in active mutants that are significantly more stable than wild type. The crystal structure of one mutant reveals that the mutant side chains pack against each other in an otherwise wild-type fold. Thus, simple hydrophobic interactions provide more stabilizing energy than the buried salt bridge and confer comparable conformational specificity.

PubMed: 7749916
DOI: 10.1038/nsb0295-122

Experimental method

X-RAY DIFFRACTION (2.4 Å)