ArticleActa crystallographica. Section D, Biological crystallography2010
Structure of the N-terminal fragment of Escherichia coli Lon protease.
Article in Acta crystallographica. Section D, Biological crystallography, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 36 citations in OpenAlex.
- Structural basis for the allosteric activation of Lon by the heat shock protein LarA.Nature communications · 2025Article
- Structure and the Mode of Activity of Lon Proteases from Diverse Organisms.Journal of molecular biology · 2022Review
- Complete three-dimensional structures of the Lon protease translocating a protein substrate.Science advances · 2021Article
- Article
- Crystal structure of XCC3289 from Xanthomonas campestris: homology with the N-terminal substrate-binding domain of Lon peptidase.Acta crystallographica. Section F, Structural biology communications · 2020Article
- Structural basis for distinct operational modes and protease activation in AAA+ protease Lon.Science advances · 2020Article
- Cryo-EM structure of substrate-freeCurrent research in structural biology · 2019Article
- New insights into structural and functional relationships between LonA proteases and ClpB chaperones.FEBS open bio · 2019Article
- Crystal structure of the N domain of Lon protease from Mycobacterium avium complex.Protein science : a publication of the Protein Society · 2019Article
- N domain of the Lon AAA+ protease controls assembly and substrate choice.Protein science : a publication of the Protein Society · 2019Article
- Defining the crucial domain and amino acid residues in bacterial Lon protease for DNA binding and processing of DNA-interacting substrates.The Journal of biological chemistry · 2017Article
- Functional characterization of LotP from Liberibacter asiaticus.Microbial biotechnology · 2017Article
- The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease.Scientific reports · 2016Article
- Mitochondrial Lon protease at the crossroads of oxidative stress, ageing and cancer.Cellular and molecular life sciences : CMLS · 2015Review
- Roles of the N domain of the AAA+ Lon protease in substrate recognition, allosteric regulation and chaperone activity.Molecular microbiology · 2014Article
- A mutation in the N domain of Escherichia coli lon stabilizes dodecamers and selectively alters degradation of model substrates.Journal of bacteriology · 2013Article
- Multitasking in the mitochondrion by the ATP-dependent Lon protease.Biochimica et biophysica acta · 2012Review
- Biological roles of the Podospora anserina mitochondrial Lon protease and the importance of its N-domain.PloS one · 2012Article
- Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
Abstract
The structure of a recombinant construct consisting of residues 1-245 of Escherichia coli Lon protease, the prototypical member of the A-type Lon family, is reported. This construct encompasses all or most of the N-terminal domain of the enzyme. The structure was solved by SeMet SAD to 2.6 A resolution utilizing trigonal crystals that contained one molecule in the asymmetric unit. The molecule consists of two compact subdomains and a very long C-terminal alpha-helix. The structure of the first subdomain (residues 1-117), which consists mostly of beta-strands, is similar to that of the shorter fragment previously expressed and crystallized, whereas the second subdomain is almost entirely helical. The fold and spatial relationship of the two subdomains, with the exception of the C-terminal helix, closely resemble the structure of BPP1347, a 203-amino-acid protein of unknown function from Bordetella parapertussis, and more distantly several other proteins. It was not possible to refine the structure to satisfactory convergence; however, since almost all of the Se atoms could be located on the basis of their anomalous scattering the correctness of the overall structure is not in question. The structure reported here was also compared with the structures of the putative substrate-binding domains of several proteins, showing topological similarities that should help in defining the binding sites used by Lon substrates.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.