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-Structure paper
Title | Structure of Geobacter cytochrome OmcZ identifies mechanism of nanowire assembly and conductivity. |
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Journal, issue, pages | Nat Microbiol, Vol. 8, Issue 2, Page 284-298, Year 2023 |
Publish date | Feb 2, 2023 |
Authors | Yangqi Gu / Matthew J Guberman-Pfeffer / Vishok Srikanth / Cong Shen / Fabian Giska / Kallol Gupta / Yuri Londer / Fadel A Samatey / Victor S Batista / Nikhil S Malvankar / |
PubMed Abstract | OmcZ nanowires produced by Geobacter species have high electron conductivity (>30 S cm). Of 111 cytochromes present in G. sulfurreducens, OmcZ is the only known nanowire-forming cytochrome ...OmcZ nanowires produced by Geobacter species have high electron conductivity (>30 S cm). Of 111 cytochromes present in G. sulfurreducens, OmcZ is the only known nanowire-forming cytochrome essential for the formation of high-current-density biofilms that require long-distance (>10 µm) extracellular electron transport. However, the mechanisms underlying OmcZ nanowire assembly and high conductivity are unknown. Here we report a 3.5-Å-resolution cryogenic electron microscopy structure for OmcZ nanowires. Our structure reveals linear and closely stacked haems that may account for conductivity. Surface-exposed haems and charge interactions explain how OmcZ nanowires bind to diverse extracellular electron acceptors and how organization of nanowire network re-arranges in different biochemical environments. In vitro studies explain how G. sulfurreducens employ a serine protease to control the assembly of OmcZ monomers into nanowires. We find that both OmcZ and serine protease are widespread in environmentally important bacteria and archaea, thus establishing a prevalence of nanowire biogenesis across diverse species and environments. |
External links | Nat Microbiol / PubMed:36732469 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 3.4 Å |
Structure data | EMDB-23481, PDB-7lq5: |
Chemicals | ChemComp-HEC: |
Source |
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Keywords | PROTEIN FIBRIL / nanowires |