spacer
spacer

PDBsum entry 1bxn

Go to PDB code: 
Top Page protein ligands Protein-protein interface(s) links
Lyase PDB id
1bxn
Jmol
Contents
Protein chains
445 a.a. *
129 a.a. *
Ligands
PO4 ×8
* Residue conservation analysis

References listed in PDB file
Key reference
Title The crystal structure of rubisco from alcaligenes eutrophus reveals a novel central eight-Stranded beta-Barrel formed by beta-Strands from four subunits.
Authors S.Hansen, V.B.Vollan, E.Hough, K.Andersen.
Ref. J Mol Biol, 1999, 288, 609-621. [DOI no: 10.1006/jmbi.1999.2701]
PubMed id 10329167
Abstract
Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) is involved in photosynthesis where it catalyzes the initial step in the fixation of carbon dioxide. The enzyme also catalyzes a competing oxygenation reaction leading to loss of fixed carbon dioxide, thus reducing the net efficiency of photosynthesis significantly. Rubisco has therefore been studied extensively, and a challenging goal is the engineering of a more photosynthetically efficient enzyme. Hexadecameric rubiscos fall in two distinct groups, "green-like" and "red-like". The ability to discriminate between CO2 and O2 as substrates varies significantly, and some algae have red-like rubisco with even higher specificity for CO2 than the plant enzyme. The structure of unactivated rubisco from Alcaligenes eutrophus has been determined to 2.7 A resolution by molecular replacement and refined to R and Rfree values of 26.6 and 32.2 %, respectively. The overall fold of the protein is very similar to the rubisco structures solved previously for green-like hexadecameric enzymes, except for the extended C-terminal domains of the small subunits which together form an eight-stranded beta-barrel which sits as a plug in the entrance to the central solvent channel in the molecule. The present structure is the first which has been solved for a red-like rubisco and is likely to represent a fold which is common for this group. The small subunits in general are believed to have a stabilizing effect, and the new quaternary structure in the oligomer of the present structure is likely to contribute even more to this stabilization of the assembled rubisco protein.
Figure 3.
Figure 3. Two dimer-related large subunits viewed down the crystallographic 2-fold axis. The backbone in one subunit is colored according to temperature factors (from dark blue for low, to red for high temperature fac- tors) and shows that the regions around the active sites are the most flexible. The essential lysine residue (Lys204) is shown in yellow. The flexible Glu207 to Met215 loop is emphasised in green. The Figure was produced with MOLSCRIPT/BOBSCRIPT (Kraulis, 1991).
Figure 10.
Figure 10. Superimposition (in stereo) of small sub- unit I of the spinach enzyme (red) on the A. eutrophus enzyme (green). The neighboring subunit J of the A. eutrophus enzyme is shown in blue. The Figure was produced with O (Jones et al., 1991).
The above figures are reprinted by permission from Elsevier: J Mol Biol (1999, 288, 609-621) copyright 1999.
Secondary reference #1
Title Purification, Crystallization and preliminary X-Ray studies of two isoforms of rubisco from alcaligenes eutrophus.
Authors S.Hansen, E.Hough, K.Andersen.
Ref. Acta Crystallogr D Biol Crystallogr, 1999, 55, 310-313. [DOI no: 10.1107/S0907444998010257]
PubMed id 10089435
Full text Abstract
Figure 1.
Figure 1 Crystals of A. eutrophus Rubisco, isoform 1. (Photograph by Gunvor Granaas, University of Tromsø.)
The above figure is reproduced from the cited reference with permission from the IUCr
PROCHECK
Go to PROCHECK summary
 Headers

 

spacer

spacer