Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme.

Abstract

Measurements of changes in structure and stability caused by 13 different substitutions for threonine 157 in phage T4 lysozyme show that the most stable lysozyme variants contain hydrogen bonds analogous to those in the wild-type enzyme and that structural adjustments allow the protein to be surprisingly tolerant of amino-acid substitutions. Study holds ProTherm entries: 1268, 1269, 1270, 1271, 1272, 1273, 1274, 1275, 1276, 1277, 1278, 1279, 1280, 1281, 13635, 13636, 13637, 13638, 13639, 13640, 13641, 13642, 13643, 13644, 13645, 13646, 13647 Extra Details: T4 lysozyme; activity; thermal stability; structure

Submission Details

ID: UQaJ5EhS

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:17 p.m.

Version: 1

Publication Details
Alber T;Sun DP;Wilson K;Wozniak JA;Cook SP;Matthews BW,Nature (1987) Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. PMID:3118211
Additional Information

Study Summary

Number of data points 41
Proteins Endolysin ; Endolysin ; Endolysin ; Endolysin ; Endolysin ; Endolysin ; Endolysin ; Endolysin ; Endolysin ; Endolysin ; Endolysin ; Endolysin ; Endolysin ; Endolysin ; Endolysin
Unique complexes 14
Assays/Quantities/Protocols Experimental Assay: ddG ; Experimental Assay: Tm ; Derived Quantity: dTm
Libraries Mutations for sequence MNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNCNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRCALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYKNL

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 UniProtKB Entries

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