4.7 Article

Cohesin-dockerin code in cellulosomal dual binding modes and its allosteric regulation by proline isomerization

期刊

STRUCTURE
卷 29, 期 6, 页码 587-+

出版社

CELL PRESS
DOI: 10.1016/j.str.2021.01.006

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资金

  1. European Union [746635]
  2. DFG excellence cluster CIPSM
  3. Seventh Framework Programme in Nanosciences, Nanotechnologies, Materials & New Production Technologies (7PM -NMP 2013-17, CellulosomePlus) [604530-2]
  4. ERA-IB-ERANET-2013-16 (FiberFuel) through Spanish MINECO [PCIN-2013-011-C02-01, EIB.12.022]
  5. MINECO/AEI/FEDER, UE [SAF2016-76678-C2-2-R]
  6. National Science Centre (NCN) [2018/31/B/NZ1/00047, 2016/21/B/NZ1/00006]
  7. Marie Curie Actions (MSCA) [746635] Funding Source: Marie Curie Actions (MSCA)

向作者/读者索取更多资源

Cellulose is a renewable and abundant organic molecule used for biofuel and chemical production. Cellulosomes, composed of multiple enzymes, display unmatched efficiency in degrading lignocellulosic substrates. By studying the cohesin-dockerin interaction, multiple binding modes and a prolyl isomerase-modulated allosteric control mechanism were discovered, providing a novel understanding of the structural plasticity and dynamics of cellulosomes.
Cellulose is the most abundant organic molecule on Earth and represents a renewable and practically everlasting feedstock for the production of biofuels and chemicals. Self-assembled owing to the high-affinity cohesin-dockerin interaction, cellulosomes are huge multi-enzyme complexes with unmatched efficiency in the degradation of recalcitrant lignocellulosic substrates. The recruitment of diverse dockerin-borne enzymes into a multicohesin protein scaffold dictates the three-dimensional layout of the complex, and interestingly two alternative binding modes have been proposed. Using single-molecule fluorescence resonance energy transfer and molecular simulations on a range of cohesin-dockerin pairs, we directly detect varying distributions between these binding modes that follow a built-in cohesin-dockerin code. Surprisingly, we uncover a prolyl isomerase-modulated allosteric control mechanism, mediated by the isomerization state of a single proline residue, which regulates the distribution and kinetics of binding modes. Overall, our data provide a novel mechanistic understanding of the structural plasticity and dynamics of cellulosomes.

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