Structural highlights
Function
[RBCX_NOSS1] An RbcL-specific chaperone. The central cleft of the RbcX homodimer (RbcX2) binds the C-terminus of an RbcL monomer, stabilizing the C-terminus and probably preventing its reassociation with chaperonin GroEL-ES. At the same time the peripheral region of RbcX2 binds a second RbcL monomer, bridging the RbcL homodimers in the correct orientation. The RbcX2(2)-bound RbcL dimers then assemble into the RbcL8 core (RbcL8-(RbcX2)8). RbcS binding triggers the release of RbcX2.[HAMAP-Rule:MF_00855] When rbcL-rbcX-rbcS or rbcL-rbcS were overexpressed in E.coli no change in reconstituted RuBisCO activity was observed, which suggests RbcX plays no role in RuBisCO assembly in this system (PubMed:8472962). However in PubMed:8472962 E.coli chaperones groL and groS were also overexpressed, which may compensate for lack of rbcX (Probable).[1] [2]
References
- ↑ Larimer FW, Soper TS. Overproduction of Anabaena 7120 ribulose-bisphosphate carboxylase/oxygenase in Escherichia coli. Gene. 1993 Apr 15;126(1):85-92. doi: 10.1016/0378-1119(93)90593-r. PMID:8472962 doi:http://dx.doi.org/10.1016/0378-1119(93)90593-r
- ↑ Onizuka T, Endo S, Akiyama H, Kanai S, Hirano M, Yokota A, Tanaka S, Miyasaka H. The rbcX gene product promotes the production and assembly of ribulose-1,5-bisphosphate carboxylase/oxygenase of Synechococcus sp. PCC7002 in Escherichia coli. Plant Cell Physiol. 2004 Oct;45(10):1390-5. doi: 10.1093/pcp/pch160. PMID:15564522 doi:http://dx.doi.org/10.1093/pcp/pch160
