3L1M

Crystal Structure of a Ni-directed Dimer of Cytochrome cb562 with a Quinolate-Histidine Hybrid Coordination Motif

Summary for 3L1M

• Entry DOI: 10.2210/pdb3l1m/pdb
• Related: 256B 2BC5 3FOO
• Descriptor: Soluble cytochrome b562, PROTOPORPHYRIN IX CONTAINING FE, N-(8-hydroxyquinolin-5-yl)acetamide, ... (5 entities in total)
• Functional Keywords: four-helix bundle, v-shaped dimer, interfacial nickel coordination, metal-binding, periplasm, transport, electron transport
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 12665.67

Authors

Radford, R.J.,Tezcan, F.A. (deposition date: 2009-12-13, release date: 2010-04-28, Last modification date: 2024-11-06)

Primary citation

Radford, R.J.,Nguyen, P.C.,Ditri, T.B.,Figueroa, J.S.,Tezcan, F.A.
Controlled protein dimerization through hybrid coordination motifs.
Inorg.Chem., 49:4362-4369, 2010

PubMed Abstract: Protein homodimerization is the simplest form of oligomerization that is frequently utilized for the construction of functional biological assemblies and the regulation of cellular pathways. Despite its simplicity, dimerization still poses an enormous challenge for protein engineering and chemical manipulation, owing to the large molecular surfaces involved in this process. We report here the construction of a hybrid coordination motif--consisting of a natural (His) and a non-natural ligand (quinolate)--on the alpha-helical surface of cytochrome cb(562), which (a) simultaneously binds divalent metals with high affinity, (b) leads to a metal-induced increase in global protein stability, and importantly, (c) enables the formation of a discrete protein dimer, whose shape is dictated by the inner-sphere metal coordination geometry and closely approximates that of the DNA-binding domains of bZIP family transcription factors.

PubMed: 20377257
DOI: 10.1021/ic100534y

Experimental method

X-RAY DIFFRACTION (2.3 Å)