5U7N

CRYSTAL STRUCTURE OF A CHIMERIC CUA DOMAIN (SUBUNIT II) OF CYTOCHROME BA3 FROM THERMUS THERMOPHILUS WITH THE AMICYANIN LOOP

Summary for 5U7N

• Entry DOI: 10.2210/pdb5u7n/pdb
• Descriptor: Cytochrome c oxidase subunit 2, COPPER (II) ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• Functional Keywords: oxidoreductase, electron transport
• Biological source: Thermus thermophilus
• Total number of polymer chains: 8
• Total formula weight: 110397.47

Authors

Otero, L.H.,Klinke, S.,Espinoza-Cara, A.,Vila, A.J. (deposition date: 2016-12-12, release date: 2017-11-22, Last modification date: 2023-10-04)

Primary citation

Espinoza-Cara, A.,Zitare, U.,Alvarez-Paggi, D.,Klinke, S.,Otero, L.H.,Murgida, D.H.,Vila, A.J.
Engineering a bifunctional copper site in the cupredoxin fold by loop-directed mutagenesis.
Chem Sci, 9:6692-6702, 2018

PubMed Abstract: Copper sites in proteins are designed to perform either electron transfer or redox catalysis. Type 1 and Cu sites are electron transfer hubs bound to a rigid protein fold that prevents binding of exogenous ligands and side reactions. Here we report the engineering of two Type 1 sites by loop-directed mutagenesis within a Cu scaffold with unique electronic structures and functional features. A copper-thioether axial bond shorter than the copper-thiolate bond is responsible for the electronic structure features, in contrast to all other natural or chimeric sites where the copper thiolate bond is short. These sites display highly unusual features, such as: (1) a high reduction potential despite a strong interaction with the axial ligand, which we attribute to changes in the hydrogen bond network and (2) the ability to bind exogenous ligands such as imidazole and azide. This strategy widens the possibility of using natural protein scaffolds with functional features not present in nature.

PubMed: 30310603
DOI: 10.1039/c8sc01444b

Experimental method

X-RAY DIFFRACTION (2.3 Å)