Crystallization (Comment) | Organism |
---|---|
urease is crystallized at 2.05 A resolution. The active-site architecture of JBU is similar to that of bacterial ureases containing a bi-nickel center. JBU has a bound phosphate and covalently modified residue (Cys592) by beta-mercaptoethanol at its active site. By correlating the structural information of JBU with the available biophysical and biochemical data on insecticidal properties of plant ureases, it is hypothesized that the amphipathic beta-hairpin located in the entomotoxic peptide region of plant ureases might form a membrane insertion beta-barrel as found in beta-poreforming toxins | Canavalia ensiformis |
Organism | UniProt | Comment | Textmining |
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Canavalia ensiformis | P07374 | - |
- |
Synonyms | Comment | Organism |
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JBU | - |
Canavalia ensiformis |
urease | - |
Canavalia ensiformis |