Comparison of metal-bound and unbound structures of aminopeptidase B proteins from Escherichia coli and Yersinia pestis.

Autor: Minasov G; Department of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.; Center for Structural Genomics of Infectious Diseases, Northwestern University, Chicago, Illinois, USA., Lam MR; Department of Molecular Biosciences, Weinberg School of Arts and Sciences, Northwestern University, Evanston, Illinois, USA., Rosas-Lemus M; Department of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.; Center for Structural Genomics of Infectious Diseases, Northwestern University, Chicago, Illinois, USA., Sławek J; Center for Structural Genomics of Infectious Diseases, Northwestern University, Chicago, Illinois, USA.; Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA., Woinska M; Center for Structural Genomics of Infectious Diseases, Northwestern University, Chicago, Illinois, USA.; Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA., Shabalin IG; Center for Structural Genomics of Infectious Diseases, Northwestern University, Chicago, Illinois, USA.; Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA., Shuvalova L; Department of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.; Center for Structural Genomics of Infectious Diseases, Northwestern University, Chicago, Illinois, USA., Palsson BØ; Department of Bioengineering and Pediatrics, University of California, San Diego, California, USA., Godzik A; Center for Structural Genomics of Infectious Diseases, Northwestern University, Chicago, Illinois, USA.; Department of Biomedical Sciences, University of California, Riverside School of Medicine, Riverside, California, USA., Minor W; Center for Structural Genomics of Infectious Diseases, Northwestern University, Chicago, Illinois, USA.; Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA., Satchell KJF; Department of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois, USA.; Center for Structural Genomics of Infectious Diseases, Northwestern University, Chicago, Illinois, USA.
Jazyk: angličtina
Zdroj: Protein science : a publication of the Protein Society [Protein Sci] 2020 Jul; Vol. 29 (7), pp. 1618-1628. Date of Electronic Publication: 2020 May 08.
DOI: 10.1002/pro.3876
Abstrakt: 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.
(© 2020 The Protein Society.)
Databáze: MEDLINE
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