Overall architecture of the SmsC<sub>2</sub>B<sub>2</sub> complex.
<p><b>(a)</b> AMP-PNP-loaded SmsC<sub>2</sub>B<sub>2</sub> crystal structure. <b>(b)</b> Close-up on the binding site of the AMP-PNP/Mg<sup>2+</sup> showing residues surrounding the binding site of AMP-PNP. <b>(c)</b> Cryo...
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2025
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| _version_ | 1852019037818585088 |
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| author | Macha Dussouchaud (21601445) |
| author2 | Markel Martinez-Carranza (21601448) Pierre-Simon Garcia (21601451) Martin Clémancey (347878) Geneviève Blondin (2668756) Jean Michel Betton (21601454) Ahmed Haouz (5624486) Simonetta Gribaldo (3252) Sandrine Ollagnier de Choudens (21601457) Ludovic Sauguet (250490) Ariel Mechaly (12131742) Frédéric Barras (207624) |
| author2_role | author author author author author author author author author author author |
| author_facet | Macha Dussouchaud (21601445) Markel Martinez-Carranza (21601448) Pierre-Simon Garcia (21601451) Martin Clémancey (347878) Geneviève Blondin (2668756) Jean Michel Betton (21601454) Ahmed Haouz (5624486) Simonetta Gribaldo (3252) Sandrine Ollagnier de Choudens (21601457) Ludovic Sauguet (250490) Ariel Mechaly (12131742) Frédéric Barras (207624) |
| author_role | author |
| dc.creator.none.fl_str_mv | Macha Dussouchaud (21601445) Markel Martinez-Carranza (21601448) Pierre-Simon Garcia (21601451) Martin Clémancey (347878) Geneviève Blondin (2668756) Jean Michel Betton (21601454) Ahmed Haouz (5624486) Simonetta Gribaldo (3252) Sandrine Ollagnier de Choudens (21601457) Ludovic Sauguet (250490) Ariel Mechaly (12131742) Frédéric Barras (207624) |
| dc.date.none.fl_str_mv | 2025-06-25T17:46:55Z |
| dc.identifier.none.fl_str_mv | 10.1371/journal.pbio.3003223.g002 |
| dc.relation.none.fl_str_mv | https://figshare.com/articles/figure/Overall_architecture_of_the_SmsC_sub_2_sub_B_sub_2_sub_complex_/29405948 |
| dc.rights.none.fl_str_mv | CC BY 4.0 info:eu-repo/semantics/openAccess |
| dc.subject.none.fl_str_mv | Biophysics Biochemistry Microbiology Genetics Biotechnology Evolutionary Biology Cancer Infectious Diseases Virology Chemical Sciences not elsewhere classified ubiquitous protein co studied modern iron present study focuses mutually exclusive allowing methanocaldococcus jannaschii </ mechanistic model describing escherichia coli </ contained cys residues bona fide </ anaerobic prokaryotes prior structural studies showed study established sms sms system rescued smsc subunit hosts suf systems grown cluster binding sites cluster assembly site biogenesis system sms biogenesis system biogenesis systems unique structural cluster assembly ancestor sms sulfur cluster unique mechanism similar c regulatory coupling nif ), key role hyperthermophilic archaeon heterotetratmer wherein gave rise functional features anoxic planet anoxic conditions |
| dc.title.none.fl_str_mv | Overall architecture of the SmsC<sub>2</sub>B<sub>2</sub> complex. |
| dc.type.none.fl_str_mv | Image Figure info:eu-repo/semantics/publishedVersion image |
| description | <p><b>(a)</b> AMP-PNP-loaded SmsC<sub>2</sub>B<sub>2</sub> crystal structure. <b>(b)</b> Close-up on the binding site of the AMP-PNP/Mg<sup>2+</sup> showing residues surrounding the binding site of AMP-PNP. <b>(c)</b> Cryo-EM structure of the [Fe-S]-bound SmsC<sub>2</sub>B<sub>2</sub> complex. <b>(d)</b> Close-up on the binding site of the [Fe-S] cluster showing the C218, C239, and C242 coordinating the [Fe-S] cluster. The cluster binding site lies in a solvent-exposed hydrophobic pocket consisting of residues P40, L216, I223, Y235, F234, and P247. <b>(e)</b> The [Fe-S] cluster-bound SmsC<sub>2</sub>B<sub>2</sub> complex exhibits asymmetry. <b>(f)</b> The [Fe-S] bound SmsC displays a folded C-terminal α-helix composed of residues 227–241 and a short terminal loop. <b>(g)</b> Close-up from the apo-SmsC-COOH region till residue 237.</p> |
| eu_rights_str_mv | openAccess |
| id | Manara_3ed4b4d37ee5c970bfb4530d47555dbe |
| identifier_str_mv | 10.1371/journal.pbio.3003223.g002 |
| network_acronym_str | Manara |
| network_name_str | ManaraRepo |
| oai_identifier_str | oai:figshare.com:article/29405948 |
| publishDate | 2025 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | CC BY 4.0 |
| spelling | Overall architecture of the SmsC<sub>2</sub>B<sub>2</sub> complex.Macha Dussouchaud (21601445)Markel Martinez-Carranza (21601448)Pierre-Simon Garcia (21601451)Martin Clémancey (347878)Geneviève Blondin (2668756)Jean Michel Betton (21601454)Ahmed Haouz (5624486)Simonetta Gribaldo (3252)Sandrine Ollagnier de Choudens (21601457)Ludovic Sauguet (250490)Ariel Mechaly (12131742)Frédéric Barras (207624)BiophysicsBiochemistryMicrobiologyGeneticsBiotechnologyEvolutionary BiologyCancerInfectious DiseasesVirologyChemical Sciences not elsewhere classifiedubiquitous protein costudied modern ironpresent study focusesmutually exclusive allowingmethanocaldococcus jannaschii </mechanistic model describingescherichia coli </contained cys residuesbona fide </anaerobic prokaryotes priorstructural studies showedstudy established smssms system rescuedsmsc subunit hostssuf systems growncluster binding sitescluster assembly sitebiogenesis system smsbiogenesis systembiogenesis systemsunique structuralcluster assemblyancestor smssulfur clusterunique mechanismsimilar cregulatory couplingnif ),key rolehyperthermophilic archaeonheterotetratmer whereingave risefunctional featuresanoxic planetanoxic conditions<p><b>(a)</b> AMP-PNP-loaded SmsC<sub>2</sub>B<sub>2</sub> crystal structure. <b>(b)</b> Close-up on the binding site of the AMP-PNP/Mg<sup>2+</sup> showing residues surrounding the binding site of AMP-PNP. <b>(c)</b> Cryo-EM structure of the [Fe-S]-bound SmsC<sub>2</sub>B<sub>2</sub> complex. <b>(d)</b> Close-up on the binding site of the [Fe-S] cluster showing the C218, C239, and C242 coordinating the [Fe-S] cluster. The cluster binding site lies in a solvent-exposed hydrophobic pocket consisting of residues P40, L216, I223, Y235, F234, and P247. <b>(e)</b> The [Fe-S] cluster-bound SmsC<sub>2</sub>B<sub>2</sub> complex exhibits asymmetry. <b>(f)</b> The [Fe-S] bound SmsC displays a folded C-terminal α-helix composed of residues 227–241 and a short terminal loop. <b>(g)</b> Close-up from the apo-SmsC-COOH region till residue 237.</p>2025-06-25T17:46:55ZImageFigureinfo:eu-repo/semantics/publishedVersionimage10.1371/journal.pbio.3003223.g002https://figshare.com/articles/figure/Overall_architecture_of_the_SmsC_sub_2_sub_B_sub_2_sub_complex_/29405948CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/294059482025-06-25T17:46:55Z |
| spellingShingle | Overall architecture of the SmsC<sub>2</sub>B<sub>2</sub> complex. Macha Dussouchaud (21601445) Biophysics Biochemistry Microbiology Genetics Biotechnology Evolutionary Biology Cancer Infectious Diseases Virology Chemical Sciences not elsewhere classified ubiquitous protein co studied modern iron present study focuses mutually exclusive allowing methanocaldococcus jannaschii </ mechanistic model describing escherichia coli </ contained cys residues bona fide </ anaerobic prokaryotes prior structural studies showed study established sms sms system rescued smsc subunit hosts suf systems grown cluster binding sites cluster assembly site biogenesis system sms biogenesis system biogenesis systems unique structural cluster assembly ancestor sms sulfur cluster unique mechanism similar c regulatory coupling nif ), key role hyperthermophilic archaeon heterotetratmer wherein gave rise functional features anoxic planet anoxic conditions |
| status_str | publishedVersion |
| title | Overall architecture of the SmsC<sub>2</sub>B<sub>2</sub> complex. |
| title_full | Overall architecture of the SmsC<sub>2</sub>B<sub>2</sub> complex. |
| title_fullStr | Overall architecture of the SmsC<sub>2</sub>B<sub>2</sub> complex. |
| title_full_unstemmed | Overall architecture of the SmsC<sub>2</sub>B<sub>2</sub> complex. |
| title_short | Overall architecture of the SmsC<sub>2</sub>B<sub>2</sub> complex. |
| title_sort | Overall architecture of the SmsC<sub>2</sub>B<sub>2</sub> complex. |
| topic | Biophysics Biochemistry Microbiology Genetics Biotechnology Evolutionary Biology Cancer Infectious Diseases Virology Chemical Sciences not elsewhere classified ubiquitous protein co studied modern iron present study focuses mutually exclusive allowing methanocaldococcus jannaschii </ mechanistic model describing escherichia coli </ contained cys residues bona fide </ anaerobic prokaryotes prior structural studies showed study established sms sms system rescued smsc subunit hosts suf systems grown cluster binding sites cluster assembly site biogenesis system sms biogenesis system biogenesis systems unique structural cluster assembly ancestor sms sulfur cluster unique mechanism similar c regulatory coupling nif ), key role hyperthermophilic archaeon heterotetratmer wherein gave rise functional features anoxic planet anoxic conditions |