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PDBsum entry 2x3h
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References listed in PDB file
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Key reference
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Title
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The k5 lyase kfla combines a viral tail spike structure with a bacterial polysaccharide lyase mechanism.
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Authors
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J.E.Thompson,
M.Pourhossein,
A.Waterhouse,
T.Hudson,
M.Goldrick,
J.P.Derrick,
I.S.Roberts.
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Ref.
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J Biol Chem, 2010,
285,
23963-23969.
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PubMed id
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Abstract
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K5 lyase A (KflA) is a tail spike protein (TSP) encoded by K5A coliphage which
cleaves K5 capsular polysaccharide, a glycosaminoglycan (GAG) with the repeat
unit [-4)-betaGlcA-(1,4)-alphaGlcNAc(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 beta-helix domain. Stable trimer formation by the intertwining of
strands in the C-terminal domain, followed by proteolytic maturation, is likely
to be catalysed 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
beta-helix fold. We propose a catalytic site and mechanism representing
convergence with the syn-beta-elimination site of heparinase II from Pedobacter
heparinus.
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