Cryo-EM structure of ATPγS-DppBCDF.
<p>(<b>A</b>) Cartoon representation of the ATPγS-DppBCDF structure. Color scheme same as in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003026#pbio.3003026.g001" target="_blank">Fig 1</a>. The EM density of ATPγS in Dp...
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2025
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| _version_ | 1852022246305955840 |
|---|---|
| author | Panpan Li (484033) |
| author2 | Manfeng Zhang (8996972) Yihua Huang (245089) |
| author2_role | author author |
| author_facet | Panpan Li (484033) Manfeng Zhang (8996972) Yihua Huang (245089) |
| author_role | author |
| dc.creator.none.fl_str_mv | Panpan Li (484033) Manfeng Zhang (8996972) Yihua Huang (245089) |
| dc.date.none.fl_str_mv | 2025-03-07T18:27:43Z |
| dc.identifier.none.fl_str_mv | 10.1371/journal.pbio.3003026.g002 |
| dc.relation.none.fl_str_mv | https://figshare.com/articles/figure/Cryo-EM_structure_of_ATP_S-DppBCDF_/28556516 |
| 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 Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified various physiological processes five distinct subunits div >< p avoiding dipeptides escaping bound dppabcdf adopts preventing dipeptide back mycobacterium tuberculosis </ dipeptide transporter dppabcdf structural studies reveal escherichia coli </ abc transporter dppabcdf bound dppbcdf adopts amppnp molecule bound coli </ complexes bound dipeptide acquisition structural observations structural characterization reveals insights reported heterotrimeric periplasm upon peptide transporters negative bacteria intracellular targets important role forth binding facing conformation em structures dppbcdf translocator dppbcd translocator binding cassette atpase subunit |
| dc.title.none.fl_str_mv | Cryo-EM structure of ATPγS-DppBCDF. |
| dc.type.none.fl_str_mv | Image Figure info:eu-repo/semantics/publishedVersion image |
| description | <p>(<b>A</b>) Cartoon representation of the ATPγS-DppBCDF structure. Color scheme same as in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003026#pbio.3003026.g001" target="_blank">Fig 1</a>. The EM density of ATPγS in DppF is shown on the right, and an ATPγS molecule is modeled in the EM density. (<b>B</b>) Structural overlay of two ATPases, DppD and DppF in ATPγS-DppBCDF showing their respective Walker A, Walker B and A loop motifs. ATPγS bound with DppF is colored violet. (<b>C</b>) ATPase activity analysis of the DppBCDF variants under different conditions. The DppBCDF was reconstituted in nanodiscs. Error bars represent mean ± SD based on three independent measurements. The data underlying this figure can be found in S1 Data.</p> |
| eu_rights_str_mv | openAccess |
| id | Manara_476f501cb2bd9cf1b2f3f978d0b4500a |
| identifier_str_mv | 10.1371/journal.pbio.3003026.g002 |
| network_acronym_str | Manara |
| network_name_str | ManaraRepo |
| oai_identifier_str | oai:figshare.com:article/28556516 |
| publishDate | 2025 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | CC BY 4.0 |
| spelling | Cryo-EM structure of ATPγS-DppBCDF.Panpan Li (484033)Manfeng Zhang (8996972)Yihua Huang (245089)BiophysicsBiochemistryMicrobiologyCell BiologyMolecular BiologyBiotechnologyBiological Sciences not elsewhere classifiedChemical Sciences not elsewhere classifiedvarious physiological processesfive distinct subunitsdiv >< pavoiding dipeptides escapingbound dppabcdf adoptspreventing dipeptide backmycobacterium tuberculosis </dipeptide transporter dppabcdfstructural studies revealescherichia coli </abc transporter dppabcdfbound dppbcdf adoptsamppnp molecule boundcoli </complexes bounddipeptide acquisitionstructural observationsstructural characterizationreveals insightsreported heterotrimericperiplasm uponpeptide transportersnegative bacteriaintracellular targetsimportant roleforth bindingfacing conformationem structuresdppbcdf translocatordppbcd translocatorbinding cassetteatpase subunit<p>(<b>A</b>) Cartoon representation of the ATPγS-DppBCDF structure. Color scheme same as in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3003026#pbio.3003026.g001" target="_blank">Fig 1</a>. The EM density of ATPγS in DppF is shown on the right, and an ATPγS molecule is modeled in the EM density. (<b>B</b>) Structural overlay of two ATPases, DppD and DppF in ATPγS-DppBCDF showing their respective Walker A, Walker B and A loop motifs. ATPγS bound with DppF is colored violet. (<b>C</b>) ATPase activity analysis of the DppBCDF variants under different conditions. The DppBCDF was reconstituted in nanodiscs. Error bars represent mean ± SD based on three independent measurements. The data underlying this figure can be found in S1 Data.</p>2025-03-07T18:27:43ZImageFigureinfo:eu-repo/semantics/publishedVersionimage10.1371/journal.pbio.3003026.g002https://figshare.com/articles/figure/Cryo-EM_structure_of_ATP_S-DppBCDF_/28556516CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/285565162025-03-07T18:27:43Z |
| spellingShingle | Cryo-EM structure of ATPγS-DppBCDF. Panpan Li (484033) Biophysics Biochemistry Microbiology Cell Biology Molecular Biology Biotechnology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified various physiological processes five distinct subunits div >< p avoiding dipeptides escaping bound dppabcdf adopts preventing dipeptide back mycobacterium tuberculosis </ dipeptide transporter dppabcdf structural studies reveal escherichia coli </ abc transporter dppabcdf bound dppbcdf adopts amppnp molecule bound coli </ complexes bound dipeptide acquisition structural observations structural characterization reveals insights reported heterotrimeric periplasm upon peptide transporters negative bacteria intracellular targets important role forth binding facing conformation em structures dppbcdf translocator dppbcd translocator binding cassette atpase subunit |
| status_str | publishedVersion |
| title | Cryo-EM structure of ATPγS-DppBCDF. |
| title_full | Cryo-EM structure of ATPγS-DppBCDF. |
| title_fullStr | Cryo-EM structure of ATPγS-DppBCDF. |
| title_full_unstemmed | Cryo-EM structure of ATPγS-DppBCDF. |
| title_short | Cryo-EM structure of ATPγS-DppBCDF. |
| title_sort | Cryo-EM structure of ATPγS-DppBCDF. |
| topic | Biophysics Biochemistry Microbiology Cell Biology Molecular Biology Biotechnology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified various physiological processes five distinct subunits div >< p avoiding dipeptides escaping bound dppabcdf adopts preventing dipeptide back mycobacterium tuberculosis </ dipeptide transporter dppabcdf structural studies reveal escherichia coli </ abc transporter dppabcdf bound dppbcdf adopts amppnp molecule bound coli </ complexes bound dipeptide acquisition structural observations structural characterization reveals insights reported heterotrimeric periplasm upon peptide transporters negative bacteria intracellular targets important role forth binding facing conformation em structures dppbcdf translocator dppbcd translocator binding cassette atpase subunit |