ArticleThe Journal of biological chemistry2010
Conserved properties of polypeptide transport-associated (POTRA) domains derived from cyanobacterial Omp85.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 55 citations in OpenAlex.
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- SAMM50 acts with p62 in piecemeal basal- and OXPHOS-induced mitophagy of SAM and MICOS components.The Journal of cell biology · 2021Article
- Protein import into chloroplasts and its regulation by the ubiquitin-proteasome system.Biochemical Society transactions · 2020Review
- Origins, function, and regulation of the TOC-TIC general protein import machinery of plastids.Journal of experimental botany · 2020Article
- Identification of a Compound That Inhibits the Growth of Gram-Negative Bacteria by Blocking BamA-BamD Interaction.Frontiers in microbiology · 2020Article
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- The TAM: A Translocation and Assembly Module of the β-Barrel Assembly Machinery in Bacterial Outer Membranes.EcoSal Plus · 2019Review
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- Structural Analysis of the Interaction between the Bacterial Cell Division Proteins FtsQ and FtsB.mBio · 2018Article
- A unified model for BAM function that takes into account type Vc secretion and species differences in BAM composition.AIMS microbiology · 2018Article
- The POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Relative Orientation of POTRA Domains from Cyanobacterial Omp85 Studied by Pulsed EPR Spectroscopy.Biophysical journal · 2016Article
- Article
- The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL Form a Trimeric Complex with Submicromolar Affinity.The Journal of biological chemistry · 2015Article
- Structure-function analysis reveals that the Pseudomonas aeruginosa Tps4 two-partner secretion system is involved in CupB5 translocation.Protein science : a publication of the Protein Society · 2015Article
- New insights into the mechanism of chloroplast protein import and its integration with protein quality control, organelle biogenesis and development.Journal of molecular biology · 2015Review
- Structure-function of cyanobacterial outer-membrane protein, Slr1270: homolog of Escherichia coli drug export/colicin import protein, TolC.FEBS letters · 2014Article
- Protein targeting and transport as a necessary consequence of increased cellular complexity.Cold Spring Harbor perspectives in biology · 2014Review
- The polypeptide transport-associated (POTRA) domains of TpsB transporters determine the system specificity of two-partner secretion systems.The Journal of biological chemistry · 2014Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins of the Omp85 family are conserved in all kingdoms of life. They mediate protein transport across or protein insertion into membranes and reside in the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts. Omp85 proteins contain a C-terminal transmembrane beta-barrel and a soluble N terminus with a varying number of polypeptide-transport-associated or POTRA domains. Here we investigate Omp85 from the cyanobacterium Anabaena sp. PCC 7120. The crystallographic three-dimensional structure of the N-terminal region shows three POTRA domains, here named P1 to P3 from the N terminus. Molecular dynamics simulations revealed a hinge between P1 and P2 but in contrast show that P2 and P3 are fixed in orientation. The P2-P3 arrangement is identical as seen for the POTRA domains from proteobacterial FhaC, suggesting this orientation is a conserved feature. Furthermore, we define interfaces for protein-protein interaction in P1 and P2. P3 possesses an extended loop unique to cyanobacteria and plantae, which influences pore properties as shown by deletion. It now becomes clear how variations in structure of individual POTRA domains, as well as the different number of POTRA domains with both rigid and flexible connections make the N termini of Omp85 proteins versatile adaptors for a plentitude of functions.
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