The K5 Lyase Kfla Combines a Viral Tail Spike Structure With a Bacterial Polysaccharide Lyase Mechanism

The K5 Lyase Kfla Combines a Viral Tail Spike Structure With a Bacterial Polysaccharide Lyase Mechanism Publisher Pubmed

Thompson JE¹ ; Pourhossein M² ; Waterhouse A¹ ; Hudson T¹ ; Goldrick M¹ ; Derrick JP¹ ; Roberts IS¹

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1. Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom
2. Department of Genetics and Molecular Biology, School of Medicine, Isfahan University of Medical Sciences, Motahhari, Yasuj 81746-73441, Iran

Source: Journal of Biological Chemistry Published:2010

Abstract

K5 lyase A (KflA) is a tail spike protein (TSP) encoded by a K5A coliphage, which cleaves K5 capsular polysaccharide, a glycosaminoglycan with the repeat unit [-4)-βGlcA-(1,4)-αGlcNAc(1-], displayed on the surface of Escherichia coli K5 strains. The crystal structure of KflA reveals a trimeric arrangement, with each monomer containing a right-handed, single-stranded parallel β-helix domain. Stable trimer formation by the intertwining of strands in the C-terminal domain, followed by proteolytic maturation, is likely to be catalyzed by an autochaperone as described for K1F endosialidase. The structure of KflA represents the first bacteriophage tail spike protein combining polysaccharide lyase activity with a single-stranded parallel β-helix fold.Wepropose a catalytic site and mechanism representing convergence with the syn-β-elimination site of heparinase II from Pedobacter heparinus. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.

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Hamid Bakherad (1)

Style	Citing Format
MLA	Thompson JE, et al.. "The K5 Lyase Kfla Combines a Viral Tail Spike Structure With a Bacterial Polysaccharide Lyase Mechanism." Journal of Biological Chemistry, vol. 285, no. 31, 2010, pp. 23963-23969.
APA	Thompson JE, Pourhossein M, Waterhouse A, Hudson T, Goldrick M, Derrick JP, Roberts IS (2010). The K5 Lyase Kfla Combines a Viral Tail Spike Structure With a Bacterial Polysaccharide Lyase Mechanism. Journal of Biological Chemistry, 285(31), 23963-23969.
Chicago	Thompson JE, Pourhossein M, Waterhouse A, Hudson T, Goldrick M, Derrick JP, Roberts IS. "The K5 Lyase Kfla Combines a Viral Tail Spike Structure With a Bacterial Polysaccharide Lyase Mechanism." Journal of Biological Chemistry 285, no. 31 (2010): 23963-23969.
Harvard	Thompson JE et al. (2010) 'The K5 Lyase Kfla Combines a Viral Tail Spike Structure With a Bacterial Polysaccharide Lyase Mechanism', Journal of Biological Chemistry, 285(31), pp. 23963-23969.
Vancouver	Thompson JE, Pourhossein M, Waterhouse A, Hudson T, Goldrick M, Derrick JP, et al.. The K5 Lyase Kfla Combines a Viral Tail Spike Structure With a Bacterial Polysaccharide Lyase Mechanism. Journal of Biological Chemistry. 2010;285(31):23963-23969.
BibTex	@article{ author = {Thompson JE and Pourhossein M and Waterhouse A and Hudson T and Goldrick M and Derrick JP and Roberts IS}, title = {The K5 Lyase Kfla Combines a Viral Tail Spike Structure With a Bacterial Polysaccharide Lyase Mechanism}, journal = {Journal of Biological Chemistry}, volume = {285}, number = {31}, pages = {23963-23969}, year = {2010} }
RIS	TY - JOUR AU - Thompson JE AU - Pourhossein M AU - Waterhouse A AU - Hudson T AU - Goldrick M AU - Derrick JP AU - Roberts IS TI - The K5 Lyase Kfla Combines a Viral Tail Spike Structure With a Bacterial Polysaccharide Lyase Mechanism JO - Journal of Biological Chemistry VL - 285 IS - 31 SP - 23963 EP - 23969 PY - 2010 ER -

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