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Evolution of a new enzyme activity from the same motif fold
Petr G Leiman1, Ian J Molineux
1Department of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, IN 47907, USA. leiman@purdue.edu
Molecular Microbiology
|April 25, 2008
Summary
Escherichia coli bacteriophage HK620 tailspike protein structure reveals similarities to related phages. This finding highlights how phages adapt protein folds for diverse host cell recognition and substrate binding.
Area of Science:
- Structural biology
- Microbiology
- Virology
Background:
- Bacteriophage HK620 tailspike is a host cell recognition protein.
- It cleaves the O18A1 type O antigen of Escherichia coli.
- Related phages P22 and Sf6 possess similar tailspikes.
Purpose of the Study:
- To determine the crystal structure of the HK620 tailspike.
- To compare its structure and organization with related phage tailspikes.
- To understand the mechanism of substrate recognition.
Main Methods:
- X-ray crystallography was used to determine the structure of the HK620 tailspike.
- Structures were determined in both apo and substrate-bound forms.
- Comparative structural analysis was performed with P22 and Sf6 tailspikes.
Main Results:
- The HK620 tailspike shares fold and organization similarities with P22 and Sf6 tailspikes despite lacking sequence similarity.
- The substrate-binding site in HK620 and P22 tailspikes is intrasubunit.
- The substrate-binding site in Sf6 tailspike is intersubunit.
Conclusions:
- Phage tailspikes can utilize similar protein folds for distinct substrate recognition mechanisms.
- Structural insights into HK620 tailspike provide a basis for understanding phage-host interactions.
- Adaptability of protein folds allows phages to evolve diverse substrate specificities.
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