PDBsum entry 1rco

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Lyase PDB id
Protein chains
(+ 2 more) 467 a.a. *
(+ 2 more) 123 a.a. *
XDP ×8
Waters ×1904
* Residue conservation analysis

References listed in PDB file
Key reference
Title A common structural basis for the inhibition of ribulose 1,5-Bisphosphate carboxylase by 4-Carboxyarabinitol 1,5-Bisphosphate and xylulose 1,5-Bisphosphate.
Authors T.C.Taylor, M.D.Fothergill, I.Andersson.
Ref. J Biol Chem, 1996, 271, 32894-32899. [DOI no: 10.1074/jbc.271.51.32894]
PubMed id 8955130
Ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the carboxylation of ribulose 1,5-bisphosphate. The reaction catalyzed by Rubisco involves several steps, some of which can occur as partial reactions, forming intermediates that can be isolated. Analogues of these intermediates are potent inhibitors of the enzyme. We have studied the interactions with the enzyme of two inhibitors, xylulose 1,5-bisphosphate and 4-carboxyarabinitol 1,5-bisphosphate, by x-ray crystallography. Crystals of the complexes were formed by cocrystallization under activating conditions. In addition, 4-carboxyarabinitol 1,5-bisphosphate was soaked into preformed activated crystals of the enzyme. The result of these experiments was the release of the activating CO2 molecule as well as the metal ion from the active site when the inhibitors bound to the enzyme. Comparison with the structure of an activated complex of the enzyme indicates that the structural basis for the release of the activator groups is a distortion of the metal binding site due to the different geometry of the C-3 hydroxyl of the inhibitors. Both inhibitors induce closure of active site loops despite the inactivated state of the enzyme. Xylulose 1,5-bisphosphate binds in a hydrated form at the active site.
Figure 1.
Fig. 1. The reactions catalyzed by Rubisco.
Figure 4.
Fig. 4. Stereochemistry of the substrate RuBP and various inhibitors of Rubisco.
The above figures are reprinted by permission from the ASBMB: J Biol Chem (1996, 271, 32894-32899) copyright 1996.
Secondary reference #1
Title Large structures at high resolution: the 1.6 a crystal structure of spinach ribulose-1,5-Bisphosphate carboxylase/oxygenase complexed with 2-Carboxyarabinitol bisphosphate.
Author I.Andersson.
Ref. J Mol Biol, 1996, 259, 160-174. [DOI no: 10.1006/jmbi.1996.0310]
PubMed id 8648644
Full text Abstract
Figure 1.
Figure 1. Reactions catalysed by rubisco.
Figure 7.
Figure 7. Overview of the active site of spinach rubisco showing 2-CABP, Mg 2+ and residues within hydrogen-bonding distance to these ligands. The hydroxyl groups at C2 and C3 of 2-CABP are in cis conformation. The two views in (a) and (b) are related by 180° with respect to the vertical axis.
The above figures are reproduced from the cited reference with permission from Elsevier
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