|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Structure of the bacterial toxin phenomycin== | | ==Structure of the bacterial toxin phenomycin== |
| - | <StructureSection load='6tkt' size='340' side='right'caption='[[6tkt]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6tkt' size='340' side='right'caption='[[6tkt]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6tkt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_biverticillatus"_preobrazhenskaya_in_gauze_et_al._1957 "actinomyces biverticillatus" preobrazhenskaya in gauze et al. 1957]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TKT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TKT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6tkt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_roseoverticillatus Streptomyces roseoverticillatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TKT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TKT FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phm ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=66429 "Actinomyces biverticillatus" Preobrazhenskaya in Gauze et al. 1957])</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6tkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tkt OCA], [https://pdbe.org/6tkt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tkt RCSB], [https://www.ebi.ac.uk/pdbsum/6tkt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tkt ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tkt OCA], [http://pdbe.org/6tkt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tkt RCSB], [http://www.ebi.ac.uk/pdbsum/6tkt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tkt ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q53805_9ACTN Q53805_9ACTN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 20: |
Line 21: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actinomyces biverticillatus preobrazhenskaya in gauze et al. 1957]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mulder, F A.A]] | + | [[Category: Streptomyces roseoverticillatus]] |
| - | [[Category: Nielsen, J T]] | + | [[Category: Mulder FAA]] |
| - | [[Category: Poulsen, T]] | + | [[Category: Nielsen JT]] |
| - | [[Category: Toerring, T]] | + | [[Category: Poulsen T]] |
| - | [[Category: Antitumor protein]] | + | [[Category: Toerring T]] |
| - | [[Category: Protein]]
| + | |
| Structural highlights
Function
Q53805_9ACTN
Publication Abstract from PubMed
Phenomycin is a bacterial mini-protein of 89 amino acids discovered more than 50 years ago with toxicity in the nanomolar regime toward mammalian cells. The protein inhibits the function of the eukaryotic ribosome in cell-free systems and appears to target translation initiation. Several fundamental questions concerning the cellular activity of phenomycin, however, have remained unanswered. In this paper, we have used morphological profiling to show that direct inhibition of translation underlies the toxicity of phenomycin in cells. We have performed studies of the cellular uptake mechanism of phenomycin, showing that endosomal escape is the toxicity-limiting step, and we have solved a solution phase high-resolution structure of the protein using NMR spectroscopy. Through bioinformatic as well as functional comparisons between phenomycin and two homologs, we have identified a peptide segment, which constitutes one of two loops in the structure that is critical for the toxicity of phenomycin.
Structure and Function of the Bacterial Protein Toxin Phenomycin.,Hansen BK, Larsen CK, Nielsen JT, Svenningsen EB, Van LB, Jacobsen KM, Bjerring M, Flygaard RK, Jenner LB, Nejsum LN, Brodersen DE, Mulder FAA, Torring T, Poulsen TB Structure. 2020 Mar 24. pii: S0969-2126(20)30075-7. doi:, 10.1016/j.str.2020.03.003. PMID:32220302[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hansen BK, Larsen CK, Nielsen JT, Svenningsen EB, Van LB, Jacobsen KM, Bjerring M, Flygaard RK, Jenner LB, Nejsum LN, Brodersen DE, Mulder FAA, Torring T, Poulsen TB. Structure and Function of the Bacterial Protein Toxin Phenomycin. Structure. 2020 Mar 24. pii: S0969-2126(20)30075-7. doi:, 10.1016/j.str.2020.03.003. PMID:32220302 doi:http://dx.doi.org/10.1016/j.str.2020.03.003
|
