S77C-ΔC7-CueR a 199mHg PAC study of the protein metal site structure /
The CueR protein regulates the cytosolic concentration of Cu(I) in bacteria such as E. coli. With this work we aimed to remodel the linear two-coordinate metal site with Cys112 and Cys120 as ligands in CueR to a tricoordinate site similar to that observed in the Hg(II) sensor protein MerR. This was...
Elmentve itt :
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| Dokumentumtípus: | Cikk |
| Megjelent: |
2024
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| Sorozat: | Interactions
245 No. 1 |
| Tárgyszavak: | |
| doi: | 10.1007/s10751-024-01879-0 |
| mtmt: | 34873932 |
| Online Access: | http://publicatio.bibl.u-szeged.hu/31948 |
| Tartalmi kivonat: | The CueR protein regulates the cytosolic concentration of Cu(I) in bacteria such as E. coli. With this work we aimed to remodel the linear two-coordinate metal site with Cys112 and Cys120 as ligands in CueR to a tricoordinate site similar to that observed in the Hg(II) sensor protein MerR. This was done by introducing an additional cysteine near the metal site in the modified S77C-ΔC7-CueR variant, inspired by the fact that Ser77 in CueR is replaced by a cysteine in MerR. 199m Hg PAC spectroscopic data indicate that two NQIs are present at pH 8.0, most likely reflecting HgS 2 and HgS 3 coordination modes, and demonstrating that the design of a pure HgS 3 metal site was not achieved. Lowering the pH to 6.0 or the temperature to −196 °C had surprisingly similar effects, giving rise to highly distorted trigonal Hg(II) coordination. Tentatively, this might reflect that the histidine just next to Cys77 (His76) coordinates forming a HgS 2 N metal site structure. Further redesign beyond the first coordination sphere appears to be required to efficiently stabilize the HgS 3 metal site structure at physiological pH. |
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| Terjedelem/Fizikai jellemzők: | 20 |
| ISSN: | 3005-0731 |