2PY8

RbcX

Summary for 2PY8

• Entry DOI: 10.2210/pdb2py8/pdb
• Descriptor: Hypothetical protein rbcX, CHLORIDE ION, 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL, ... (4 entities in total)
• Functional Keywords: all helical fold, chaperone
• Biological source: Synechocystis sp. PCC 6803
• Total number of polymer chains: 4
• Total formula weight: 67552.52

Authors

Tanaka, S.,Sawaya, M.R.,Kerfeld, C.A.,Yeates, T.O. (deposition date: 2007-05-15, release date: 2007-10-09, Last modification date: 2024-02-21)

Primary citation

Tanaka, S.,Sawaya, M.R.,Kerfeld, C.A.,Yeates, T.O.
Structure of the RuBisCO chaperone RbcX from Synechocystis sp. PCC6803.
Acta Crystallogr.,Sect.D, 63:1109-1112, 2007

PubMed Abstract: 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.

PubMed: 17881829
DOI: 10.1107/S090744490704228X

Experimental method

X-RAY DIFFRACTION (2.45 Å)