{"doi":"10.1002/pro.3876","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>","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.","journal":"Protein Science","year":2020,"id":111706,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":4,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.9229,"is_data_producer":false,"deposit_databanks":null,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2020-01-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":530934,"name":"Matthew R. Lam","orcid":null,"position":1,"is_corresponding":false},{"id":493829,"name":"Mónica Rosas‐Lemus","orcid":"0000-0002-6243-0271","position":2,"is_corresponding":false},{"id":530034,"name":"Joanna Sławek","orcid":"0000-0002-1754-2741","position":3,"is_corresponding":false},{"id":530035,"name":"M. Woińska","orcid":"0000-0002-9956-5356","position":4,"is_corresponding":false},{"id":530935,"name":"Ivan G. Shabalin","orcid":null,"position":5,"is_corresponding":false},{"id":530036,"name":"L. Shuvalova","orcid":"0000-0003-1702-6998","position":6,"is_corresponding":false},{"id":5441,"name":"Bernhard Ø. Palsson","orcid":"0000-0003-2357-6785","position":7,"is_corresponding":false},{"id":12333,"name":"Adam Godzik","orcid":"0000-0002-2425-852X","position":8,"is_corresponding":false},{"id":17727,"name":"W. Minor","orcid":"0000-0001-7075-7090","position":9,"is_corresponding":false},{"id":36778,"name":"Karla J. F. Satchell","orcid":"0000-0003-3274-7611","position":10,"is_corresponding":false},{"id":530033,"name":"G. Minasov","orcid":"0000-0001-5460-3462","position":0,"is_corresponding":true}],"reference_count":40,"raw_metadata":null,"created_at":"2026-07-18T23:13:09.353152Z","pmid":"32306515","pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}