Structural comparison of urease and a GroEL analog from Helicobacter pylori.
Electron microscopy of purified protein preparations indicated that Helicobacter pylori urease consisted of circular particles that are 13 nm in diameter, some of which showed indications of threefold rotational symmetry. A GroEL analog of H. pylori (Hp60K) appeared as a disc-shaped molecule with a diameter similar to that of urease but possessed sevenfold rotational symmetry. In a side-view projection, Hp60K appeared as two or four discs stacked side by side.
Department of Biochemistry and Microbiology, University of Victoria, British Columbia, Canada.
J W
JW
Austin
P
P
Doig
M
M
Stewart
T J
TJ
Trust
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000648:ultrastructure*; D018834:Chaperonin 60; D004591:Electrophoresis, Polyacrylamide Gel; D006360:Heat-Shock Proteins / Q000302:isolation & purification / Q000648:ultrastructure*; D016480:Helicobacter pylori / Q000201:enzymology / Q000378:metabolism*; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D008970:Molecular Weight; D017386:Sequence Homology, Amino Acid; D014510:Urease / Q000302:isolation & purification / Q000648:ultrastructure*
C078096:60K protein, Helicobacter pylori; D001426:Bacterial Proteins; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D014510:Urease