6GRI

E. coli Microcin synthetase McbBCD complex

Summary for 6GRI

• Entry DOI: 10.2210/pdb6gri/pdb
• Descriptor: Microcin B17-processing protein McbB, Microcin B17-processing protein McbC, Microcin B17-processing protein McbD, ... (8 entities in total)
• Functional Keywords: microcin, dna gyrase, heterocyclization, posttranslational modification, biosynthetic protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 4
• Total formula weight: 144703.40

Authors

Ghilarov, D.,Stevenson, C.E.M.,Travin, D.Y.,Piskunova, J.,Serebryakova, M.,Maxwell, A.,Lawson, D.M.,Severinov, K. (deposition date: 2018-06-11, release date: 2019-01-30, Last modification date: 2024-01-17)

Primary citation

Ghilarov, D.,Stevenson, C.E.M.,Travin, D.Y.,Piskunova, J.,Serebryakova, M.,Maxwell, A.,Lawson, D.M.,Severinov, K.
Architecture of Microcin B17 Synthetase: An Octameric Protein Complex Converting a Ribosomally Synthesized Peptide into a DNA Gyrase Poison.
Mol. Cell, 73:749-762.e5, 2019

PubMed Abstract: The introduction of azole heterocycles into a peptide backbone is the principal step in the biosynthesis of numerous compounds with therapeutic potential. One of them is microcin B17, a bacterial topoisomerase inhibitor whose activity depends on the conversion of selected serine and cysteine residues of the precursor peptide to oxazoles and thiazoles by the McbBCD synthetase complex. Crystal structures of McbBCD reveal an octameric BCD complex with two bound substrate peptides. Each McbB dimer clamps the N-terminal recognition sequence, while the C-terminal heterocycle of the modified peptide is trapped in the active site of McbC. The McbD and McbC active sites are distant from each other, which necessitates alternate shuttling of the peptide substrate between them, while remaining tethered to the McbB dimer. An atomic-level view of the azole synthetase is a starting point for deeper understanding and control of biosynthesis of a large group of ribosomally synthesized natural products.

PubMed: 30661981
DOI: 10.1016/j.molcel.2018.11.032

Experimental method

X-RAY DIFFRACTION (2.7 Å)