Structural insights into higher order assembly and function of the bacterial micro compartment protein PduA

Allan Pang; Stefanie Frank; Ian R. Brown; Martin J. Warren; Richard W. Pickersgill

doi:10.1074/jbc.M114.569285

Structural insights into higher order assembly and function of the bacterial micro compartment protein PduA

Allan Pang, Stefanie Frank, Ian R. Brown, Martin J. Warren, Richard W. Pickersgill

Faculty of Science

Research output: Contribution to journal › Article › peer-review

62 Citations (Scopus)

Abstract

Background: PduA is a major shell protein in 1,2-propanediol utilization micro compartments. Results: The profound influence of Lys-26 and Arg-79 on hexagonal tiling is revealed both in the crystal and in vivo. Conclusion: Interactions seen in the crystal are important for sheet and nanotube assembly in the bacterial cytoplasm. Significance: This work provides knowledge for the engineering of PduA for stability and porosity for synthetic biology applications.

Original language	English
Pages (from-to)	22377-22384
Number of pages	8
Journal	Journal of Biological Chemistry
Volume	289
Issue number	32
DOIs	https://doi.org/10.1074/jbc.M114.569285
Publication status	Published - 8 Aug 2014

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10.1074/jbc.M114.569285Licence: CC BY

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Structural insights into higher order assembly and function of the bacterial micro compartment protein PduA

Abstract

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