6NLU

Circularly permuted Haliangium ochraceum BMC-H

Summary for 6NLU

• Entry DOI: 10.2210/pdb6nlu/pdb
• Descriptor: circularly permuted BMC-H (2 entities in total)
• Functional Keywords: bacterial microcompartment, structural protein
• Biological source: Haliangium ochraceum; More
• Total number of polymer chains: 2
• Total formula weight: 21118.21

Authors

Sutter, M.,Ferlez, B.,Kerfeld, C.A. (deposition date: 2019-01-09, release date: 2019-05-22, Last modification date: 2023-10-11)

Primary citation

Ferlez, B.,Sutter, M.,Kerfeld, C.A.
A designed bacterial microcompartment shell with tunable composition and precision cargo loading.
Metab. Eng., 54:286-291, 2019

PubMed Abstract: Microbes often augment their metabolism by conditionally constructing proteinaceous organelles, known as bacterial microcompartments (BMCs), that encapsulate enzymes to degrade organic compounds or assimilate CO. BMCs self-assemble and are spatially delimited by a semi-permeable shell made up of hexameric, trimeric, and pentameric shell proteins. Bioengineers aim to recapitulate the organization and efficiency of these complex biological architectures by redesigning the shell to incorporate non-native enzymes from biotechnologically relevant pathways. To meet this challenge, a diverse set of synthetic biology tools are required, including methods to manipulate the properties of the shell as well as target and organize cargo encapsulation. We designed and determined the crystal structure of a synthetic shell protein building block with an inverted sidedness of its N- and C-terminal residues relative to its natural counterpart; the inversion targets genetically fused protein cargo to the lumen of the shell. Moreover, the titer of fluorescent protein cargo encapsulated using this strategy is controllable using an inducible tetracycline promoter. These results expand the available set of building blocks for precision engineering of BMC-based nanoreactors and are compatible with orthogonal methods which will facilitate the installation and organization of multi-enzyme pathways.

PubMed: 31075444
DOI: 10.1016/j.ymben.2019.04.011

Experimental method

X-RAY DIFFRACTION (1.607 Å)