Identification of TesA as the periplasmic partner of YbbAP.
<p><b>(A)</b> Pairwise <i><i>in silico</i></i> co-folding of YbbP with all sec/tat secreted proteins from <i><i>Escherichia coli</i></i>. Each co-fold attempt is represented on the 2D plot by their pDockQ score and Molprobity clash sc...
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2025
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| _version_ | 1849927626430349312 |
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| author | Martin B. L. McAndrew (22683641) |
| author2 | Jonathan Cook (3435386) Amy Gill (14910614) Kavya Sahoo (22683644) Clare Thomas (7943747) Phillip J. Stansfeld (1267617) Allister Crow (263807) |
| author2_role | author author author author author author |
| author_facet | Martin B. L. McAndrew (22683641) Jonathan Cook (3435386) Amy Gill (14910614) Kavya Sahoo (22683644) Clare Thomas (7943747) Phillip J. Stansfeld (1267617) Allister Crow (263807) |
| author_role | author |
| dc.creator.none.fl_str_mv | Martin B. L. McAndrew (22683641) Jonathan Cook (3435386) Amy Gill (14910614) Kavya Sahoo (22683644) Clare Thomas (7943747) Phillip J. Stansfeld (1267617) Allister Crow (263807) |
| dc.date.none.fl_str_mv | 2025-11-25T18:40:13Z |
| dc.identifier.none.fl_str_mv | 10.1371/journal.pbio.3003427.g001 |
| dc.relation.none.fl_str_mv | https://figshare.com/articles/figure/Identification_of_TesA_as_the_periplasmic_partner_of_YbbAP_/30714857 |
| dc.rights.none.fl_str_mv | CC BY 4.0 info:eu-repo/semantics/openAccess |
| dc.subject.none.fl_str_mv | Biophysics Biochemistry Microbiology Cell Biology Molecular Biology Biotechnology Developmental Biology Cancer Hematology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified Information Systems not elsewhere classified tolc efflux pump multifunctional hydrolytic enzyme extracts hydrophobic compounds extracting hydrophobic molecules capture implied long bacterial cell envelope active site residues lipid hydrolase complex escherichia coli </ data suggests ybbap abc superfamily ’ div >< p coli </ abc superfamily thioester substrates tesa complex structural characterization remarkable diversity new function mechanotransmission mechanism inner membrane extensively characterized experimentally confirm complete ybbap >, three |
| dc.title.none.fl_str_mv | Identification of TesA as the periplasmic partner of YbbAP. |
| dc.type.none.fl_str_mv | Image Figure info:eu-repo/semantics/publishedVersion image |
| description | <p><b>(A)</b> Pairwise <i><i>in silico</i></i> co-folding of YbbP with all sec/tat secreted proteins from <i><i>Escherichia coli</i></i>. Each co-fold attempt is represented on the 2D plot by their pDockQ score and Molprobity clash score. The TesA-YbbP pair is indicated. <b>(B)</b> Genomic arrangement of YbbA, YbbP, TesA, and YbbO genes in <i><i>E. coli</i></i>. <b>(C)</b> Coevolution analysis between YbbP and TesA. All inter-protein residues were scored for coevolution using CCMPred, converted to a Z-score, and depicted as a frequency histogram. Coevolving residue pairs between YbbP and TesA with Z-scores above 10 are annotated (Further coevolving residue pairs within the YbbAP-TesA complex are given in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003427#pbio.3003427.s001" target="_blank">S1 Table</a>). <b>(D)</b> SDS-PAGE gel showing co-purification of YbbAP-TesA as a complex. Underlying data can be found in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003427#pbio.3003427.s018" target="_blank">S1 Data</a>–<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003427#pbio.3003427.s020" target="_blank">S3 Data</a>.</p> |
| eu_rights_str_mv | openAccess |
| id | Manara_0f544be03f9fb0108c39df45422bd6ce |
| identifier_str_mv | 10.1371/journal.pbio.3003427.g001 |
| network_acronym_str | Manara |
| network_name_str | ManaraRepo |
| oai_identifier_str | oai:figshare.com:article/30714857 |
| publishDate | 2025 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | CC BY 4.0 |
| spelling | Identification of TesA as the periplasmic partner of YbbAP.Martin B. L. McAndrew (22683641)Jonathan Cook (3435386)Amy Gill (14910614)Kavya Sahoo (22683644)Clare Thomas (7943747)Phillip J. Stansfeld (1267617)Allister Crow (263807)BiophysicsBiochemistryMicrobiologyCell BiologyMolecular BiologyBiotechnologyDevelopmental BiologyCancerHematologyBiological Sciences not elsewhere classifiedChemical Sciences not elsewhere classifiedInformation Systems not elsewhere classifiedtolc efflux pumpmultifunctional hydrolytic enzymeextracts hydrophobic compoundsextracting hydrophobic moleculescapture implied longbacterial cell envelopeactive site residueslipid hydrolase complexescherichia coli </data suggests ybbapabc superfamily ’div >< pcoli </abc superfamilythioester substratestesa complexstructural characterizationremarkable diversitynew functionmechanotransmission mechanisminner membraneextensively characterizedexperimentally confirmcomplete ybbap>, three<p><b>(A)</b> Pairwise <i><i>in silico</i></i> co-folding of YbbP with all sec/tat secreted proteins from <i><i>Escherichia coli</i></i>. Each co-fold attempt is represented on the 2D plot by their pDockQ score and Molprobity clash score. The TesA-YbbP pair is indicated. <b>(B)</b> Genomic arrangement of YbbA, YbbP, TesA, and YbbO genes in <i><i>E. coli</i></i>. <b>(C)</b> Coevolution analysis between YbbP and TesA. All inter-protein residues were scored for coevolution using CCMPred, converted to a Z-score, and depicted as a frequency histogram. Coevolving residue pairs between YbbP and TesA with Z-scores above 10 are annotated (Further coevolving residue pairs within the YbbAP-TesA complex are given in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003427#pbio.3003427.s001" target="_blank">S1 Table</a>). <b>(D)</b> SDS-PAGE gel showing co-purification of YbbAP-TesA as a complex. Underlying data can be found in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003427#pbio.3003427.s018" target="_blank">S1 Data</a>–<a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003427#pbio.3003427.s020" target="_blank">S3 Data</a>.</p>2025-11-25T18:40:13ZImageFigureinfo:eu-repo/semantics/publishedVersionimage10.1371/journal.pbio.3003427.g001https://figshare.com/articles/figure/Identification_of_TesA_as_the_periplasmic_partner_of_YbbAP_/30714857CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/307148572025-11-25T18:40:13Z |
| spellingShingle | Identification of TesA as the periplasmic partner of YbbAP. Martin B. L. McAndrew (22683641) Biophysics Biochemistry Microbiology Cell Biology Molecular Biology Biotechnology Developmental Biology Cancer Hematology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified Information Systems not elsewhere classified tolc efflux pump multifunctional hydrolytic enzyme extracts hydrophobic compounds extracting hydrophobic molecules capture implied long bacterial cell envelope active site residues lipid hydrolase complex escherichia coli </ data suggests ybbap abc superfamily ’ div >< p coli </ abc superfamily thioester substrates tesa complex structural characterization remarkable diversity new function mechanotransmission mechanism inner membrane extensively characterized experimentally confirm complete ybbap >, three |
| status_str | publishedVersion |
| title | Identification of TesA as the periplasmic partner of YbbAP. |
| title_full | Identification of TesA as the periplasmic partner of YbbAP. |
| title_fullStr | Identification of TesA as the periplasmic partner of YbbAP. |
| title_full_unstemmed | Identification of TesA as the periplasmic partner of YbbAP. |
| title_short | Identification of TesA as the periplasmic partner of YbbAP. |
| title_sort | Identification of TesA as the periplasmic partner of YbbAP. |
| topic | Biophysics Biochemistry Microbiology Cell Biology Molecular Biology Biotechnology Developmental Biology Cancer Hematology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified Information Systems not elsewhere classified tolc efflux pump multifunctional hydrolytic enzyme extracts hydrophobic compounds extracting hydrophobic molecules capture implied long bacterial cell envelope active site residues lipid hydrolase complex escherichia coli </ data suggests ybbap abc superfamily ’ div >< p coli </ abc superfamily thioester substrates tesa complex structural characterization remarkable diversity new function mechanotransmission mechanism inner membrane extensively characterized experimentally confirm complete ybbap >, three |