Characterization of the structure and catalytic activity of Legionella pneumophila VipF
| Autor: | Christopher E. Berndsen, Tracy A. Caldwell, Byron H. Young, Oleksandr Kokhan, Aidan M. McKenzie |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Legionella Protein domain Gene Expression Sequence alignment Molecular Dynamics Simulation Biochemistry Legionella pneumophila Protein Structure Secondary Conserved sequence Substrate Specificity 03 medical and health sciences Structure-Activity Relationship Bacterial Proteins Protein Domains Structural Biology Acetyl Coenzyme A Acetyltransferases Catalytic Domain Escherichia coli Homology modeling Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence Conserved Sequence 030102 biochemistry & molecular biology biology Chemistry biology.organism_classification Recombinant Proteins Kinetics 030104 developmental biology Chloramphenicol Docking (molecular) Structural Homology Protein Sequence Alignment Plasmids |
| Zdroj: | Proteins. 84(10) |
| ISSN: | 1097-0134 |
| Popis: | The pathogenic bacteria Legionella pneumophila is known to cause Legionnaires' Disease, a severe pneumonia that can be fatal to immunocompromised individuals and the elderly. Shohdy et al. identified the L. pneumophila vacuole sorting inhibitory protein VipF as a putative N-acetyltransferase based on sequence homology. We have characterized the basic structural and functional properties of VipF to confirm this original functional assignment. Sequence conservation analysis indicates two putative CoA-binding regions within VipF. Homology modeling and small angle X-ray scattering suggest a monomeric, dual-domain structure joined by a flexible linker. Each domain contains the characteristic beta-splay motif found in many acetyltransferases, suggesting that VipF may contain two active sites. Docking experiments suggest reasonable acetyl-CoA binding locations within each beta-splay motif. Broad substrate screening indicated that VipF is capable of acetylating chloramphenicol and both domains are catalytically active. Given that chloramphenicol is not known to be N-acetylated, this is a surprising finding suggesting that VipF is capable of O-acetyltransferase activity. Proteins 2016; 84:1422-1430. © 2016 Wiley Periodicals, Inc. |
| Databáze: | OpenAIRE |
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