Comparison of metal-bound and unbound structures of aminopeptidase B proteins from Escherichia coli and Yersinia pestis
| Autor: | Minasov, George, Lam, Matthew R, Rosas-Lemus, Monica, Sławek, Joanna, Woinska, Magdalena, Shabalin, Ivan G, Shuvalova, Ludmilla, Palsson, Bernhard Ø, Godzik, Adam, Minor, Wladek, Satchell, Karla JF |
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| Rok vydání: | 2020 |
| Předmět: |
Manganese
Crystallography aminopeptidase metalloprotease Yersinia pestis Escherichia coli Proteins PepB Biophysics Computation Theory and Mathematics Aminopeptidases Vector-Borne Diseases Zinc Emerging Infectious Diseases Protein Domains Escherichia coli X-Ray hexamer Biochemistry and Cell Biology Other Information and Computing Sciences X-ray crystallography |
| Zdroj: | Protein science : a publication of the Protein Society, vol 29, iss 7 |
| Popis: | Protein degradation by aminopeptidases is involved in bacterial responses to stress. Escherichia coli produces two metal-dependent M17 family leucine aminopeptidases (LAPs), aminopeptidase A (PepA) and aminopeptidase B (PepB). Several structures have been solved for PepA as well as other bacterial M17 peptidases. Herein, we report the first structures of a PepB M17 peptidase. The E. coli PepB protein structure was determined at a resolution of 2.05 and 2.6 Å. One structure has both Zn2+ and Mn2+ , while the second structure has two Zn2+ ions bound to the active site. A 2.75 Å apo structure is also reported for PepB from Yersinia pestis. Both proteins form homohexamers, similar to the overall arrangement of PepA and other M17 peptidases. However, the divergent N-terminal domain in PepB is much larger resulting in a tertiary structure that is more expanded. Modeling of a dipeptide substrate into the C-terminal LAP domain reveals contacts that account for PepB to uniquely cleave after aspartate. |
| Databáze: | OpenAIRE |
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