8QBQ
Crystal structure of the outer membrane decaheme cytochrome MtrC (A430Boc-Lys)
Summary for 8QBQ
| Entry DOI | 10.2210/pdb8qbq/pdb |
| Related | 4LM8 |
| Descriptor | Extracellular iron oxide respiratory system surface decaheme cytochrome c component MtrC, 1,2-ETHANEDIOL, ACETATE ION, ... (6 entities in total) |
| Functional Keywords | boc-lys, cytochrome, electron transport., electron transport |
| Biological source | Shewanella oneidensis MR-1 |
| Total number of polymer chains | 1 |
| Total formula weight | 79788.03 |
| Authors | Nash, B.W.,Lockwood, C.J.,Whiting, K.,Butt, J.N.,Clarke, T.A.,Edwards, M.J. (deposition date: 2023-08-25, release date: 2024-09-04, Last modification date: 2024-10-02) |
| Primary citation | Lockwood, C.W.J.,Nash, B.W.,Newton-Payne, S.E.,van Wonderen, J.H.,Whiting, K.P.S.,Connolly, A.,Sutton-Cook, A.L.,Crook, A.,Aithal, A.R.,Edwards, M.J.,Clarke, T.A.,Sachdeva, A.,Butt, J.N. Genetic Code Expansion in Shewanella oneidensis MR-1 Allows Site-Specific Incorporation of Bioorthogonal Functional Groups into a c -Type Cytochrome. Acs Synth Biol, 13:2833-2843, 2024 Cited by PubMed Abstract: Genetic code expansion has enabled cellular synthesis of proteins containing unique chemical functional groups to allow the understanding and modulation of biological systems and engineer new biotechnology. Here, we report the development of efficient methods for site-specific incorporation of structurally diverse noncanonical amino acids (ncAAs) into proteins expressed in the electroactive bacterium MR-1. We demonstrate that the biosynthetic machinery for ncAA incorporation is compatible and orthogonal to the endogenous pathways of MR-1 for protein synthesis, maturation of -type cytochromes, and protein secretion. This allowed the efficient synthesis of a -type cytochrome, MtrC, containing site-specifically incorporated ncAA in MR-1 cells. We demonstrate that site-specific replacement of surface residues in MtrC with ncAAs does not influence its three-dimensional structure and redox properties. We also demonstrate that site-specifically incorporated bioorthogonal functional groups could be used for efficient site-selective labeling of MtrC with fluorophores. These synthetic biology developments pave the way to expand the chemical repertoire of designer proteins expressed in MR-1. PubMed: 39158169DOI: 10.1021/acssynbio.4c00248 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.81 Å) |
Structure validation
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