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TitleScaffolding protein CcmM directs multiprotein phase separation in β-carboxysome biogenesis.
Journal, issue, pagesNat Struct Mol Biol, Vol. 28, Issue 11, Page 909-922, Year 2021
Publish dateNov 10, 2021
AuthorsKun Zang / Huping Wang / F Ulrich Hartl / Manajit Hayer-Hartl /
PubMed AbstractCarboxysomes in cyanobacteria enclose the enzymes Rubisco and carbonic anhydrase to optimize photosynthetic carbon fixation. Understanding carboxysome assembly has implications in agricultural ...Carboxysomes in cyanobacteria enclose the enzymes Rubisco and carbonic anhydrase to optimize photosynthetic carbon fixation. Understanding carboxysome assembly has implications in agricultural biotechnology. Here we analyzed the role of the scaffolding protein CcmM of the β-cyanobacterium Synechococcus elongatus PCC 7942 in sequestrating the hexadecameric Rubisco and the tetrameric carbonic anhydrase, CcaA. We find that the trimeric CcmM, consisting of γCAL oligomerization domains and linked small subunit-like (SSUL) modules, plays a central role in mediation of pre-carboxysome condensate formation through multivalent, cooperative interactions. The γCAL domains interact with the C-terminal tails of the CcaA subunits and additionally mediate a head-to-head association of CcmM trimers. Interestingly, SSUL modules, besides their known function in recruiting Rubisco, also participate in intermolecular interactions with the γCAL domains, providing further valency for network formation. Our findings reveal the mechanism by which CcmM functions as a central organizer of the pre-carboxysome multiprotein matrix, concentrating the core components Rubisco and CcaA before β-carboxysome shell formation.
External linksNat Struct Mol Biol / PubMed:34759380 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.63 - 8.0 Å
Structure data

EMDB-12730:
SSUL-gCAL mediating Synechococcus elongatus PCC 7942 M58 homo-demixing
Method: EM (single particle) / Resolution: 3.57 Å

EMDB-12731:
Structure of the repeat unit in the network formed by CcmM full length isoform and Rubisco from Synechococcus elongatus
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-12732:
CryoEM structure of the interaction between CcmM full length isoform (SSUL) domain with RbcL8 core from Synechococcus elongatus PCC 7942
Method: EM (single particle) / Resolution: 8.0 Å

PDB-7o4z:
Crystal structure of the carbonic anhydrase-like domain of CcmM from Synechococcus elongatus (strain PCC 7942)
Method: X-RAY DIFFRACTION / Resolution: 1.67 Å

PDB-7o54:
Crystal structure of the carbonic anhydrase-like domain of CcmM in complex with the C-terminal 17 residues of CcaA from Synechococcus elongatus (strain PCC 7942)
Method: X-RAY DIFFRACTION / Resolution: 1.63 Å

Chemicals

ChemComp-NI:
NICKEL (II) ION / Nickel

ChemComp-CL:
Unknown entry / Chloride

ChemComp-HOH:
WATER / Water

Source
  • Synechococcus elongatus PCC 7942 = FACHB-805 (bacteria)
  • synechococcus elongatus (strain pcc 7942 / fachb-805) (bacteria)
KeywordsPHOTOSYNTHESIS / protein binding carboxysome

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