3HNJ

Crystal structure of the Zn-induced tetramer of the engineered cyt cb562 variant RIDC-2

Summary for 3HNJ

• Entry DOI: 10.2210/pdb3hnj/pdb
• Related: 2BC5 2QLA 3HNI 3HNK 3HNL
• Descriptor: Soluble cytochrome b562, PROTOPORPHYRIN IX CONTAINING FE, ZINC ION, ... (4 entities in total)
• Functional Keywords: electron transport, metal binding protein
• Biological source: Escherichia coli
• Cellular location: Periplasm: P0ABE7
• Total number of polymer chains: 4
• Total formula weight: 49657.99

Authors

Salgado, E.N.,Lewis, R.A.,Brodin, J.,Tezcan, F.A. (deposition date: 2009-05-31, release date: 2010-02-09, Last modification date: 2023-09-06)

Primary citation

Salgado, E.N.,Ambroggio, X.I.,Brodin, J.D.,Lewis, R.A.,Kuhlman, B.,Tezcan, F.A.
Metal templated design of protein interfaces.
Proc.Natl.Acad.Sci.USA, 107:1827-1832, 2010

PubMed Abstract: Metal coordination is a key structural and functional component of a large fraction of proteins. Given this dual role we considered the possibility that metal coordination may have played a templating role in the early evolution of protein folds and complexes. We describe here a rational design approach, Metal Templated Interface Redesign (MeTIR), that mimics the time course of a hypothetical evolutionary pathway for the formation of stable protein assemblies through an initial metal coordination event. Using a folded monomeric protein, cytochrome cb(562), as a building block we show that its non-self-associating surface can be made self-associating through a minimal number of mutations that enable Zn coordination. The protein interfaces in the resulting Zn-directed, D(2)-symmetrical tetramer are subsequently redesigned, yielding unique protein architectures that self-assemble in the presence or absence of metals. Aside from its evolutionary implications, MeTIR provides a route to engineer de novo protein interfaces and metal coordination environments that can be tuned through the extensive noncovalent bonding interactions in these interfaces.

PubMed: 20080561
DOI: 10.1073/pnas.0906852107

Experimental method

X-RAY DIFFRACTION (2 Å)