NMR evidence for independent domain structures in zoocin A, an antibacterial exoenzyme

NMR was used to obtain spectroscopic evidence supporting a two domain model for zoocin A in which an N-terminal catalytic domain is linked by a threonine–proline rich linker to a target recognition domain responsible for recognizing the cell wall of bacteria susceptible to the bacteriolytic action o...

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Published inBiochemical and biophysical research communications Vol. 317; no. 2; pp. 527 - 530
Main Authors Liang, Qiaoli, Simmonds, Robin S., Timkovich, Russell
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 30.04.2004
Subjects
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - classification
Bacterial Proteins - chemistry
Bacterial Proteins - classification
Bacteriolytic
Catalysis
Endopeptidase
Enzyme Activation
Lysostaphin
Magnetic Resonance Spectroscopy - methods
NMR
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Structure-Activity Relationship
Zoocin
Lysostaphin
NMR
Zoocin
Bacteriolytic
Endopeptidase
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Summary:NMR was used to obtain spectroscopic evidence supporting a two domain model for zoocin A in which an N-terminal catalytic domain is linked by a threonine–proline rich linker to a target recognition domain responsible for recognizing the cell wall of bacteria susceptible to the bacteriolytic action of the enzyme. When cloned and separately expressed, each domain retains the folding found in the whole enzyme. Additionally, spectroscopy suggests that the target recognition domain has a conformation typical of a soluble globular protein, while the catalytic domain aggregates at low millimolar concentrations.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2004.03.088