2x3h | pdb_00002x3h

COLIPHAGE K5A LYASE

spinqualitylabelsall models 2x3h, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2x3h is a 3 chain structure with sequence from Bacteriophage k1-5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BR Activity: Heparin lyase, with EC number 4.2.2.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. The K5 lyase KflA combines a viral tail spike structure with a bacterial polysaccharide lyase mechanism.,Thompson JE, Pourhossein M, Waterhouse A, Hudson T, Goldrick M, Derrick JP, Roberts IS J Biol Chem. 2010 Jul 30;285(31):23963-9. Epub 2010 Jun 2. PMID:20519506 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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