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. 2007 Nov 7;129(44):13374-5.
doi: 10.1021/ja075261o. Epub 2007 Oct 12.

Controlling protein-protein interactions through metal coordination: assembly of a 16-helix bundle protein

Eric N Salgado  1 , Jasmin Faraone-Mennella, F Akif Tezcan
Affiliations

Controlling protein-protein interactions through metal coordination: assembly of a 16-helix bundle protein

Eric N Salgado et al. J Am Chem Soc. .
No abstract available

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Figures

Figure 1
Figure 1
Crystal structure of the 4 Zn-4 His4-cb562 assembly. Pairs of protein molecules that form the V-shaped dimers are colored alike. Zn ions are shown as grey spheres. (a) View of the assembly parallel to the non-crystallographic twofold axis and the corresponding cylindrical representation of Helix 3's involved in Zn coordination; (b) view down the non-crystallographic twofold axis; (c) close-up view of the Zn coordination environment and simulated-annealing Fo-Fc omit electron density map (grey, 4σ; purple, 12σ). The parent molecules for metal ligands are shown in subscripts.
Figure 2
Figure 2
Molecular mass distributions of His4-cb562 species determined by sedimentation velocity experiments. The distributions are normalized with respect to the area covered under the curves.
See this image and copyright information in PMC

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