Structure of the RuBisCO chaperone RbcX from Synechocystis sp. PCC6803.
In some cyanobacteria, the genes for the large and small subunits of the enzyme RuBisCO are separated on the bacterial chromosome by the insertion of a gene coding for a protein designated RbcX, which acts as a chaperone for RuBisCO. A recent structural study [Saschenbrecker et al. (2007), Cell, 129, 1189-1200] has shed light on the mechanism by which RbcX assists RuBisCO assembly. Here, the crystal structure of RbcX from another cyanobacterium, Synechocystis sp. PCC6803, is reported, revealing an unusually long protruding C-terminal helix, as well as a bound polyethylene glycol molecule in the protein substrate-binding site.
Tanaka
Shiho
S
UCLA Department of Chemistry and Biochemistry, 611 Charles Young Drive East, Los Angeles, CA 90095-1569, USA.
Sawaya
Michael R
MR
Kerfeld
Cheryl A
CA
Yeates
Todd O
TO
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D001665:Binding Sites; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray / Q000379:methods; D000458:Cyanobacteria / Q000378:metabolism; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism*; D008969:Molecular Sequence Data; D011092:Polyethylene Glycols / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D001426:Bacterial Proteins; D018832:Molecular Chaperones; C522129:RbcX protein, cyanobacteria; D011092:Polyethylene Glycols; D012273:Ribulose-Bisphosphate Carboxylase