v5.1.0.3
Glycine data from LIS
Type | Family |
Description | The RbcX protein has been identified as having a chaperonin-like function as it assists in the correct assembly of RbcL and RbcS subunits during RuBisCO biogenesis and it is also required to reach its maximal activity [ , ]. The rbcX gene is juxtaposed to and cotranscribed with rbcL and rbcS encoding RubisCO in Anabaena sp. (strain CA / ATCC 33047) []. Crystal structure studies revealed that RbcX is composed almost exclusively of α-helices, which form an unusual four-helix bundle. Additionally, all known RbcX proteins exist as homodimers (RbcX2). The central cleft of this homodimer binds the C-terminal of a RbcL monomer, stabilizing it, and the peripheral region of RbcX2 binds a second RbcL monomer, which allows the RbcL homodimers to be in the correct orientation []. |
Short Name | Chaperonin_RcbX |