ArticleProceedings of the National Academy of Sciences of the United States of America2006
Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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47 citing papers in PubMed, 114 citations in OpenAlex.
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- LifeSoaks: a tool for analyzing solvent channels in protein crystals and obstacles for soaking experiments.Acta crystallographica. Section D, Structural biology · 2023Article
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- X-ray crystal structure and specificity of the Toxoplasma gondii ME49 TgAPN2.The Biochemical journal · 2020Article
- High Genetic Potential for Proteolytic Decomposition in Northern Peatland Ecosystems.Applied and environmental microbiology · 2019Article
- Zn-dependent bifunctional proteases are responsible for leader peptide processing of class III lanthipeptides.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Aminobenzosuberone Scaffold as a Modular Chemical Tool for the Inhibition of Therapeutically Relevant M1 Aminopeptidases.Molecules (Basel, Switzerland) · 2018Article
- Discovery of novel non-competitive inhibitors of mammalian neutral M1 aminopeptidase (APN).Biochimie · 2017Article
- Biochemical characterization of aminopeptidase N2 from Toxoplasma gondii.The Journal of veterinary medical science · 2017Article
- Allosteric inhibition of aminopeptidase N functions related to tumor growth and virus infection.Scientific reports · 2017Article
- An overview of heavy-atom derivatization of protein crystals.Acta crystallographica. Section D, Structural biology · 2016Review
- Structural basis for the inhibition of M1 family aminopeptidases by the natural product actinonin: Crystal structure in complex with E. coli aminopeptidase N.Protein science : a publication of the Protein Society · 2015Article
- Structure-guided, single-point modifications in the phosphinic dipeptide structure yield highly potent and selective inhibitors of neutral aminopeptidases.Journal of medicinal chemistry · 2014Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aminopeptidase N from Escherichia coli is a major metalloprotease that participates in the controlled hydrolysis of peptides in the proteolytic pathway. Determination of the 870-aa structure reveals that it has four domains similar to the tricorn-interacting factor F3. The thermolysin-like active site is enclosed within a large cavity with a volume of 2,200 A(3), which is inaccessible to substrates except for a small opening of approximately 8-10 A. The substrate-based inhibitor bestatin binds to the protein with minimal changes, suggesting that this is the active form of the enzyme. The previously described structure of F3 had three distinct conformations that were described as "closed," "intermediate," and "open." The structure of aminopeptidase N from E. coli, however, is substantially more closed than any of these. Taken together, the results suggest that these proteases, which are involved in intracellular peptide degradation, prevent inadvertent hydrolysis of inappropriate substrates by enclosing the active site within a large cavity. There is also some evidence that the open form of the enzyme, which admits substrates, remains inactive until it adopts the closed form.
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