Tailspike protein mutant E372Q of E. coli bacteriophage HK620

Single Amino Acid Exchange in Bacteriophage Hk620 Tailspike Protein Results in Thousand-Fold Increase of its Oligosaccharide Affinity.

Crystal Structure of Escherichia Coli Phage Hk620 Tailspike: Podoviral Tailspike Endoglycosidase Modules are Evolutionarily Related.

PROTEIN WAS CRYSTALLISED FROM 3.5 M SODIUMFORMATE, 0.1 M TRIS-HCL, PH 8.5.

TAILSPIKE PROTEIN OF E.COLI BACTERIOPHAGE HK620

TAILSPIKE PROTEIN OF E.COLI BACTERIOPHAGE HK620 IN COMPLEX WITH HEXASACCHARIDE

TAILSPIKE PROTEIN MUTANT E372Q OF E.COLI BACTERIOPHAGE HK620 IN COMPLEX WITH HEXASACCHARIDE

TAILSPIKE PROTEIN MUTANT D339N OF E.COLI BACTERIOPHAGE HK620 IN COMPLEX WITH HEXASACCHARIDE

TAILSPIKE PROTEIN MUTANT D339A OF E.COLI BACTERIOPHAGE HK620 IN COMPLEX WITH HEXASACCHARIDE

TAILSPIKE PROTEIN OF E. COLI BACTERIOPHAGE HK620 IN COMPLEX WITH HEXASACCHARIDE

SHEET
THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
TWO SHEETS ARE DEFINED.

ENGINEERED RESIDUE IN CHAIN A, GLU 373 TO GLN

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

VIRAL PROTEIN, ENDO-N-ACETYLGLUCOSAMINIDASE, O-ANTIGEN