The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme.


Abstract

To understand better how the packing of side chains within the core influences protein structure and stability, the crystal structures were determined for eight variants of T4 lysozyme, each of which contains three to five substitutions at adjacent interior sites. Concerted main-chain and side-chain displacements, with movements of helical segments as large as 0.8 angstrom, were observed. In contrast, the angular conformations of the mutated side chains tended to remain unchanged, with torsion angles within 20 degrees of those in the wild-type structure. These observations suggest that not only the rotation of side chains but also movements of the main chain must be considered in the evaluation of which amino acid sequences are compatible with a given protein fold. Study holds ProTherm entries: 1162, 1163, 1164, 1165, 1166, 1167, 1168, 1169, 1170, 13570, 13571, 13572, 13573, 13574, 13575, 13576, 13577 Extra Details: ddG was measured at 51.5 degrees C T4 lysozyme; flexibility; protein structure; packing

Submission Details

ID: 5w4oMFC

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:16 p.m.

Version: 1

Publication Details
Baldwin EP;Hajiseyedjavadi O;Baase WA;Matthews BW,Science (1993) The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme. PMID:8259514
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