The structure of neutral protease from Bacillus cereus at 0.2-nm resolution.
The crystal structure of the neutral protease from Bacillus cereus has been refined to an R factor of 17.5% at 0.2-nm resolution. The enzyme, an extracellular metalloendopeptidase, consists of two domains and binds one zinc and four calcium ions. The structure is very similar to that of thermolysin, with which the enzyme shares 73% amino-acid sequence identity. The active-site cleft between the two domains is wider in neutral protease than in thermolysin. This suggests the presence of a flexible hinge region between the two domains, which may assist enzyme action. The high-resolution analysis allows detailed examination of possible causes for the difference in thermostability between neutral protease and thermolysin.
Stark
W
W
Department of Structural Biology, University of Basel, Switzerland.
Pauptit
R A
RA
Wilson
K S
KS
Jansonius
J N
JN
D000595:Amino Acid Sequence; D001409:Bacillus cereus / Q000201:enzymology*; D001665:Binding Sites; D002118:Calcium / Q000737:chemistry; D003461:Crystallography; D006358:Hot Temperature; D006860:Hydrogen Bonding; D008666:Metalloendopeptidases / Q000737:chemistry / Q000648:ultrastructure*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015260:Neprilysin / Q000737:chemistry / Q000648:ultrastructure; D011487:Protein Conformation; D011489:Protein Denaturation; D016415:Sequence Alignment; D013696:Temperature; D013820:Thermolysin / Q000737:chemistry / Q000648:ultrastructure; D014961:X-Ray Diffraction; D015032:Zinc / Q000737:chemistry
D008666:Metalloendopeptidases; C044194:microbial metalloproteinases; D015260:Neprilysin; D013820:Thermolysin; D015032:Zinc; D002118:Calcium