Domains in lambda Cro repressor. A calorimetric study.


Abstract

Thermodynamic properties of a mutant lambda Cro repressor with Cys replacing Val55 were studied calorimetrically. Formation of the S-S cross-link between neighboring Cys55 residues in this dimeric molecule leads to stabilization of a structure formed by the C-terminal parts of the two polypeptide chains, which behave as a single cooperative domain upon protein denaturation by heating. This composite domain is very stable at neutral pH and disrupts at 110 degrees C. The S-S-cross-linked tryptic fragment (residues 22-66), which includes this C-terminal domain, has similar stability. The N-terminal parts of the polypeptide chains do not form any stable structure when isolated, but in S-S-cross-linked dimer, they form a single cooperative block which melts in an all-or-none way 9 degrees C higher than the un-cross-linked protein. The observed cooperation of the distant N-terminal parts in dimer raises questions regarding lambda Cro repressor structure in solution. Study holds ProTherm entries: 5311, 5312, 5313, 5314, 5315, 5316, 5317, 5318, 5319 Extra Details: dimeric molecule; single cooperative domain; S-S-cross-linked

Submission Details

ID: zDqzXLgE

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:29 p.m.

Version: 1

Publication Details
Griko YV;Rogov VV;Privalov PL,Biochemistry (1992) Domains in lambda Cro repressor. A calorimetric study. PMID:1472508
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
2ORC 1998-05-27 CRO REPRESSOR INSERTION MUTANT K56-[DGEVK], NMR, 32 STRUCTURES
2A63 2006-06-06 Solution structure of a stably monomeric mutant of lambda Cro produced by substitutions in the ball-and-socket interface
1COP 1995-10-15 THREE-DIMENSIONAL DIMER STRUCTURE OF THE LAMBDA-CRO REPRESSOR IN SOLUTION AS DETERMINED BY HETERONUCLEAR MULTIDIMENSIONAL NMR
2OVG 2008-01-08 1.35 Lambda Cro Q27P/A29S/K32Q triple mutant at 1.35 A in space group P3221
2ECS 2008-01-08 1.4 Lambda Cro mutant Q27P/A29S/K32Q at 1.4 A in space group C2
1ORC 1996-12-23 1.54 CRO REPRESSOR INSERTION MUTANT K56-[DGEVK]
1D1M 1999-09-24 2.05 CRYSTAL STRUCTURE OF CRO K56-[DGEVK]-F58W MUTANT
1D1L 1999-10-06 2.1 CRYSTAL STRUCTURE OF CRO-F58W MUTANT
5CRO 1998-06-17 2.3 REFINED STRUCTURE OF CRO REPRESSOR PROTEIN FROM BACTERIOPHAGE LAMBDA
3ORC 1998-12-02 3.0 CRYSTAL STRUCTURE OF AN ENGINEERED CRO MONOMER BOUND NONSPECIFICALLY TO DNA
6CRO 1998-09-18 3.0 CRYSTAL STRUCTURE OF LAMBDA-CRO BOUND TO A CONSENSUS OPERATOR AT 3.0 ANGSTROM RESOLUTION
4CRO 1992-01-15 3.9 PROTEIN-DNA CONFORMATIONAL CHANGES IN THE CRYSTAL STRUCTURE OF A LAMBDA CRO-OPERATOR COMPLEX

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Regulatory protein cro P03040 RCRO_LAMBD