2X3H

COLIPHAGE K5A LYASE

2X3H の概要

• エントリーDOI: 10.2210/pdb2x3h/pdb
• 分子名称: K5 LYASE, BROMIDE ION (3 entities in total)
• 機能のキーワード: lyase, bacteriophage, glycosaminoglycan
• 由来する生物種: ENTEROBACTERIA PHAGE K1-5
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 170089.41

構造登録者

Thompson, J.E.,Pourhossein, M.,Goldrick, M.,Hudson, T.,Derrick, J.P.,Roberts, I.S. (登録日: 2010-02-04, 公開日: 2010-06-02, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.6 Å)