1L11

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME

Summary for 1L11

• Entry DOI: 10.2210/pdb1l11/pdb
• Related: 1L01 1L02 1L03 1L04 1L05 1L06 1L07 1L08 1L09 1L10 1L12 1L13 1L14 1L15 1L16 1L17 1L18 1L19 1L20 1L21 1L22 1L23 1L24 1L25 1L26 1L27 1L28 1L29 1L30 1L31 1L32 1L33 1L34 1L35 1L36 2LZM
• Descriptor: T4 LYSOZYME, BETA-MERCAPTOETHANOL (3 entities in total)
• Functional Keywords: hydrolase (o-glycosyl)
• Biological source: Enterobacteria phage T4
• Cellular location: Host cytoplasm : P00720
• Total number of polymer chains: 1
• Total formula weight: 18752.65

Authors

Dao-Pin, S.,Wilson, K.,Alber, T.,Matthews, B.W. (deposition date: 1988-02-05, release date: 1988-04-16, Last modification date: 2022-11-23)

Primary citation

Alber, T.,Sun, D.P.,Wilson, K.,Wozniak, J.A.,Cook, S.P.,Matthews, B.W.
Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme.
Nature, 330:41-46, 1987

PubMed 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.

PubMed: 3118211
DOI: 10.1038/330041a0

Experimental method

X-RAY DIFFRACTION (1.7 Å)