2X3H

COLIPHAGE K5A LYASE

Summary for 2X3H

• Entry DOI: 10.2210/pdb2x3h/pdb
• Descriptor: K5 LYASE, BROMIDE ION (3 entities in total)
• Functional Keywords: lyase, bacteriophage, glycosaminoglycan
• Biological source: ENTEROBACTERIA PHAGE K1-5
• Total number of polymer chains: 3
• Total formula weight: 170089.41

Authors

Thompson, J.E.,Pourhossein, M.,Goldrick, M.,Hudson, T.,Derrick, J.P.,Roberts, I.S. (deposition date: 2010-02-04, release date: 2010-06-02, Last modification date: 2024-05-08)

Primary citation

Thompson, J.E.,Pourhossein, M.,Waterhouse, A.,Hudson, T.,Goldrick, M.,Derrick, J.P.,Roberts, I.S.
The K5 Lyase Kfla Combines a Viral Tail Spike Structure with a Bacterial Polysaccharide Lyase Mechanism.
J.Biol.Chem., 285:23963-, 2010

PubMed 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)-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 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 beta-helix fold. We propose a catalytic site and mechanism representing convergence with the syn-beta-elimination site of heparinase II from Pedobacter heparinus.

PubMed: 20519506
DOI: 10.1074/JBC.M110.127571

Experimental method

X-RAY DIFFRACTION (1.6 Å)