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- W3016583921 abstract "Abstract 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 Zn 2+ and Mn 2+ , while the second structure has two Zn 2+ 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." @default.
- W3016583921 created "2020-04-24" @default.
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- W3016583921 date "2020-05-08" @default.
- W3016583921 modified "2023-10-06" @default.
- W3016583921 title "Comparison of metal‐bound and unbound structures of aminopeptidase B proteins from <scp> <i>Escherichia coli</i> </scp> and <scp> <i>Yersinia pestis</i> </scp>" @default.
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- W3016583921 doi "https://doi.org/10.1002/pro.3876" @default.
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