Abstract

BcsD is broadly present throughout Proteobacteria and is predicted to contribute to cellulose crystallinity via interaction with BcsH. However, new work shows that, in non-crystalline forming Proteobacteria, BcsD contains an amino-terminal a1-helix, forms a tetrahedron-like structure, and interacts with alternative proline-rich protein partners.

Original languageEnglish
Pages (from-to)R69-R72
JournalCurrent Biology
Volume34
Issue number2
DOIs
StatePublished - Jan 22 2024

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