1rco
From Proteopedia
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| - | [[Image:1rco.gif|left|200px]]<br /> | + | [[Image:1rco.gif|left|200px]]<br /><applet load="1rco" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1rco" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1rco, resolution 2.3Å" /> | caption="1rco, resolution 2.3Å" /> | ||
'''SPINACH RUBISCO IN COMPLEX WITH THE INHIBITOR D-XYLULOSE-2,2-DIOL-1,5-BISPHOSPHATE'''<br /> | '''SPINACH RUBISCO IN COMPLEX WITH THE INHIBITOR D-XYLULOSE-2,2-DIOL-1,5-BISPHOSPHATE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RCO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea] with XDP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] | + | 1RCO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea] with XDP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] Known structural/functional Sites: <scene name='pdbsite=ACB:Active Site'>ACB</scene>, <scene name='pdbsite=ACE:Active Site'>ACE</scene>, <scene name='pdbsite=ACH:Active Site'>ACH</scene>, <scene name='pdbsite=ACK:Active Site'>ACK</scene>, <scene name='pdbsite=ACL:Active Site'>ACL</scene>, <scene name='pdbsite=ACO:Active Site'>ACO</scene>, <scene name='pdbsite=ACR:Active Site'>ACR</scene> and <scene name='pdbsite=ACV:Active Site'>ACV</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RCO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:59:04 2007'' |
Revision as of 15:49, 18 December 2007
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SPINACH RUBISCO IN COMPLEX WITH THE INHIBITOR D-XYLULOSE-2,2-DIOL-1,5-BISPHOSPHATE
Overview
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.
About this Structure
1RCO is a Protein complex structure of sequences from Spinacia oleracea with XDP as ligand. Active as Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 Known structural/functional Sites: , , , , , , and . Full crystallographic information is available from OCA.
Reference
A common structural basis for the inhibition of ribulose 1,5-bisphosphate carboxylase by 4-carboxyarabinitol 1,5-bisphosphate and xylulose 1,5-bisphosphate., Taylor TC, Fothergill MD, Andersson I, J Biol Chem. 1996 Dec 20;271(51):32894-9. PMID:8955130
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