Ribulose-1,5-bisphosphate carboxylase/oxygenase
From Proteopedia
"LEU332 INFLUENCES THE CO2/O2 SPECIFICITY FACTOR OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE OXYGENASE FROM ANACYSTIS NIDULANS" G.J. Lee, K.A. McDonald, and B.A. McFadden
Contents of file LEE.KIN: Kin.1 - Animation of activated/unactivated tobacco RuBisCO active site sidechains Kin.2 - Animation of loop 6 movement between activated & unactivated tobacco RuBisCO
(KineMage currently not supported)
Kinemage 1 is an animation comparing the active sites of activated and unactivated tobacco RuBisCO. Leu335, the corresponding mutation site in tobacco, is highlighted, as well as other sidechains of interest. Glu60, a mechanistically-involved sidechain, and Asn123, a potential metal ion ligand, are contributed by the neighboring L subunit (subunit 2). CABP, activator CO2, and Mg2+, associated with the activated form of the enzyme, are displayed. Also shown are mainchain atoms for residues 380, 381 and 402-404, which are known to be involved in mainchain hydrogen bonding with the substrate. Note the movement (approx. 11 Å relative to the hydroxyl moiety of Ser379) of the Leu335 gamma carbon towards the active site, suggesting a role for Leu335 in controlling access of the substrate, RuBP, to the active site. Stereoviewing is recommended with view2. The corresponding residue numbers for the Anacystis nidulans enzyme are 3 less than those indicated for the tobacco enzyme.
Kinemage 2 is an animation of the motion of loop 6 of activated and unactivated RuBisCO from tobacco. Calpha traces from positions 324-348 with Leu335 are shown; conserved Lys334 and His327, which bind opposite phosphates in CABP, can also be highlighted. CABP and Mg2+, bound in the activated form of the enzyme, are displayed. Stereoviewing is recommended with view2. The corresponding residue numbers for the Anacystis nidulans enzyme are 3 less than those indicated for the tobacco enzyme.
Coordinates from Brookhaven Data Bank files: 3RUB (tobacco, unactivated), 4RUB (tobacco, activated)
Additional Resources
For additional information, see: Photosynthesis
3D structures of RuBisCO
References
Unactivated form: Curmi, P.M.G., Cascio, D., Sweet, R.M., Eisenberg, D.S., & Schreuder, H. (1992). Crystal structure of the unactivated form of ribulose-1,5-bisphosphate carboxylase/oxygenase from tobacco refined at 2.0-A resolution. J. Biol. Chem. 267, 16980-16989. Activated, CABP-bound form: Eisenberg, D.S. (see Schreuder, et al., this issue).
