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3TOM

Crystal structure of an engineered cytochrome cb562 that forms 2D, Zn-mediated sheets

Summary for 3TOM
Entry DOI10.2210/pdb3tom/pdb
Related2BC5 2QLA 3TOL
DescriptorSoluble cytochrome b562, PROTOPORPHYRIN IX CONTAINING FE, ZINC ION, ... (4 entities in total)
Functional Keywordsfour helix bundle, electron transfer, periplasmic space, metal binding protein
Biological sourceEscherichia coli
Cellular locationPeriplasm: P0ABE7
Total number of polymer chains4
Total formula weight49386.89
Authors
Brodin, J.B.,Tezcan, F.A. (deposition date: 2011-09-05, release date: 2012-07-04, Last modification date: 2024-02-28)
Primary citationBrodin, J.D.,Ambroggio, X.I.,Tang, C.,Parent, K.N.,Baker, T.S.,Tezcan, F.A.
Metal-directed, chemically tunable assembly of one-, two- and three-dimensional crystalline protein arrays.
Nat Chem, 4:375-382, 2012
Cited by
PubMed Abstract: Proteins represent the most sophisticated building blocks available to an organism and to the laboratory chemist. Yet, in contrast to nearly all other types of molecular building blocks, the designed self-assembly of proteins has largely been inaccessible because of the chemical and structural heterogeneity of protein surfaces. To circumvent the challenge of programming extensive non-covalent interactions to control protein self-assembly, we have previously exploited the directionality and strength of metal coordination interactions to guide the formation of closed, homoligomeric protein assemblies. Here, we extend this strategy to the generation of periodic protein arrays. We show that a monomeric protein with properly oriented coordination motifs on its surface can arrange, on metal binding, into one-dimensional nanotubes and two- or three-dimensional crystalline arrays with dimensions that collectively span nearly the entire nano- and micrometre scale. The assembly of these arrays is tuned predictably by external stimuli, such as metal concentration and pH.
PubMed: 22522257
DOI: 10.1038/nchem.1290
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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