User:Nikhil Malvankar/Cytochrome nanowires

Interactive 3D Complement in Proteopedia

Structure of Microbial Nanowires Reveals Stacked Hemes that Transport Electrons over Micrometers.

Fengbin Wang, Yanqui Gu, J. Patrick O'Brien, Sophia M. Yi, Sibel Ebru Yalcin, Vishok Srikanth, Cong Shen, Dennis Vu, Nicole L. Ing, Allon I. Hochbaum, Edward H. Egelman, and Nikhil S. Malvankar. Cell 177:361-9, April 4, 2019. doi:10.1016/j.cell.2019.03.029

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Background The electrically conductive nanowires that extend from cells of Geobacter sulfurreducens have long been thought to be pili assembled from PilA protein. However, the evidence was indirect. Here, the structure of filaments of wild type Geobacter sulfurreducens, confirmed to be electrically conductive, was determined by cryo-electron microscopy (6ef8). Surprisingly, these nanowires are assembled from outer membrane cytochrome OmcS. These findings were confirmed a short time later (6nef). Nanowire Structure A nanowire model composed of 7 OmcS protein chains, each shown a different color, was constructed from the 3.2-3.7 Å cryo-EM density (). The filament is ~4 nm in diamater, and has a characteristic undulating or sinusoidal form with a wavelength (pitch) of ~20 nm. The OmcS monomers have 407 amino acids each. The .  Amino Terminus                 Carboxy Terminus  The amino terminus forms a bulge that fits into the slightly concave carboxy-terminal face of the contacting subunit. OmcS Structure The OmcS monomer has . Alpha Helices, 310 Helices,  Beta Strands ,  Loops . The structure assigned by the authors is 77% loops; Jmol objectively assigns 82% loops. The authors assigned 10% alpha helices, 7% 310 helices, and 6% beta strands. The OmcS structure determined by Filman et al. was very similar, with 80% loops assigned by the authors (86% by Jmol), having only 3% beta strand but otherwise very similar. We compared OmcS with three other c-type multi-heme cytochrome crystal structures: 1ofw, 3ucp, and 3ov0 had 45%, 49%, and 60% loops respectively. Hemes Each OmcS monomer : C O N Fe. The hemes are arranged in parallel-displaced pairs. Each pair is orthogonal to the next pair. The , which likely contributes to the stability of the filament. More importantly, this produces a . This continuous chain of hemes is believed to be the basis of the electrical conductivity. Cysteine Anchors Each heme is , which form thioether bonds with the heme vinyl groups (opposite the heme carboxyls): C O N S Fe. 12 CxxCH motifs in the OmcS sequence anchor the 6 hemes within each OmcS chain. Histidine to Iron Each heme , in addition to the four heme nitrogens. The iron of heme 5 (the next to last heme at the carboxy end of the chain) is bound to His 332 from its own chain (Chain A), and His 16 in the N-terminal "bulge" of the next protein chain (Chain B) in the filament. This inter-chain histidine-iron bond is undoubtedly important in strengthening the monomer-monomer interfaces in the filament. The histidines bound to hemes 1, 2, 3, 4, and 6 are all in the same protein chain that contains those hemes.

spinqualitylabelsall models Geobacter sulfurreducens outer membrane cytochrome S (OmcS) 6ef8. Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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• Malvankar: A list of all interactive 3D complements for publications from the Malvankar group.