Circular permutation of T4 lysozyme.


Abstract

To examine the relationship between polypeptide chain synthesis and protein folding, we have constructed a circularly permuted variant of phage T4 lysozyme. The permuted protein begins at residue 37 of the wild-type sequence and ends at residue 36. The normal chain termini are joined by a six-residue linker, Ser-Gly4-Ala. The permuted lysozyme folds efficiently and cleaves bacterial cell walls with normal specific activity. As judged by circular dichroism, UV absorbance, fluorescence, and nuclear magnetic resonance spectroscopy, the permutation causes little change in the structure of the protein. Reversible denaturation experiments show that the permutation reduces the stability of T4 lysozyme only 0.8-1.1 kcal/mol. These results demonstrate that a protein with two domains can be permuted with little change in activity, structure, and stability. The order of chain synthesis, the sequential arrangement of secondary structures, and the position of chain termini with respect to domain boundaries do not determine the protein fold. Study holds ProTherm entries: 4625, 4626, 4627, 4628, 4629 Extra Details: circular permutation; specific activity; sequential arrangement;,secondary structures

Submission Details

ID: dUDmzWUr

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:26 p.m.

Version: 1

Publication Details
Zhang T;Bertelsen E;Benvegnu D;Alber T,Biochemistry (1993) Circular permutation of T4 lysozyme. PMID:8241117
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
102L 1992-09-29T00:00:00+0000 1.74 HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME
103L 1992-09-29T00:00:00+0000 1.9 HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME
104L 1992-09-29T00:00:00+0000 2.8 HOW AMINO-ACID INSERTIONS ARE ALLOWED IN AN ALPHA-HELIX OF T4 LYSOZYME
107L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
108L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
109L 1992-12-17T00:00:00+0000 1.85 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
110L 1992-12-17T00:00:00+0000 1.7 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
111L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
112L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME
113L 1992-12-17T00:00:00+0000 1.8 STRUCTURAL BASIS OF ALPHA-HELIX PROPENSITY AT TWO SITES IN T4 LYSOZYME

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Endolysin P00720 ENLYS_BPT4