Overall architecture of the SmsC<sub>2</sub>B<sub>2</sub> complex.

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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Main Author: Macha Dussouchaud (21601445) (author)
Other Authors: Markel Martinez-Carranza (21601448) (author), Pierre-Simon Garcia (21601451) (author), Martin Clémancey (347878) (author), Geneviève Blondin (2668756) (author), Jean Michel Betton (21601454) (author), Ahmed Haouz (5624486) (author), Simonetta Gribaldo (3252) (author), Sandrine Ollagnier de Choudens (21601457) (author), Ludovic Sauguet (250490) (author), Ariel Mechaly (12131742) (author), Frédéric Barras (207624) (author)
Published: 2025
Subjects:
Biophysics
Biochemistry
Microbiology
Genetics
Biotechnology
Evolutionary Biology
Cancer
Infectious Diseases
Virology
Chemical Sciences not elsewhere classified
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anoxic conditions
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Summary:<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>

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