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The structure, kinetics and interactions of the β-carboxysomal β-carbonic anhydrase, CcaA.

Biochem. J.. 2016-12; 
McGurnLeah D,Moazami-GoudarziMaryam,WhiteSean A,SuwalTannu,BrarBeant,TangJason Q,EspieGeorge S,KimberMatth
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Custom Vector Construction The nucleotide sequences encoding CcaA274 (822 bp) and CcmM206-4A (621 bp) from Synechocystis sp. PCC 6803 were synthesized by GenScript (Piscataway, NJ) and subsequently cloned into the NdeI or BamHI-HindIII restriction site of the pET-28b expression vector. Get A Quote

摘要

CcaA is a β-carbonic anhydrase (CA) that is a component of the carboxysomes of a subset of β-cyanobacteria. This protein, which has a characteristic C-terminal extension of unknown function, is recruited to the carboxysome via interactions with CcmM, which is itself a γ-CA homolog with enzymatic activity in many, but not all cyanobacteria. We have determined the structure of CcaA from Synechocystis sp. PCC 6803 at 1.45 Å. In contrast with the dimer-of-dimers organization of most bacterial β-CAs, or the loose dimer-of-dimers-of-dimers organization found in the plant enzymes, CcaA shows a well-packed trimer-of-dimers organization. The proximal part of the characteristic C-terminal extension is ... More

关键词

bacterial microcompartments,carbon dioxide-concentrating mechanism,carbonic anhydrase,carboxysomes,cyanobacteria,photosynth