@article{4c7c9e31d0284f32ab1bfee620ec3eae,
title = "Comparison of metal-bound and unbound structures of aminopeptidase B proteins from Escherichia coli and Yersinia pestis",
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 {\AA}. One structure has both Zn2+ and Mn2+, while the second structure has two Zn2+ ions bound to the active site. A 2.75 {\AA} 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.",
keywords = "Escherichia coli, PepB, X-ray crystallography, Yersinia pestis, aminopeptidase, hexamer, metalloprotease",
author = "George Minasov and Lam, {Matthew R.} and Monica Rosas-Lemus and Joanna S{\l}awek and Magdalena Woinska and Shabalin, {Ivan G.} and Ludmilla Shuvalova and Bernhard Palsson and Adam Godzik and Wladek Minor and Satchell, {Karla J.F.}",
note = "Funding Information: The authors thank Marin Cymborowski, Sarah Grimshaw, Lukasz Jaroszewski, Olga Kiryukhina, Keewhon Kwon, Nathan Mih, Zdzislaw Warwzak, and James Windsor for target selection, cloning, crystallization, and protein purification, as well as for assistance in solving the structures. This project has been funded in whole or in part with Federal funds from the National Institute of Allergy and Infectious Diseases, National Institutes of Health, Department of Health and Human Services, under Contract Nos. HHSN272201200026C and HHSN272201700060C and under Grant No. U01AI124316. M. R. L. was funded by an Undergraduate Research Fellowship from Northwestern University. Funding Information: Undergraduate Research Fellowship from Northwestern University; National Institute of Allergy and Infectious Diseases, National Institutes of Health, Grant/Award Numbers: HHSN272201200026C, HHSN272201700060C, U01AI124316 Funding information Publisher Copyright: {\textcopyright} 2020 The Protein Society",
year = "2020",
month = jul,
day = "1",
doi = "10.1002/pro.3876",
language = "English (US)",
volume = "29",
pages = "1618--1628",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Cold Spring Harbor Laboratory Press",
number = "7",
}