1rsc
From Proteopedia
| Line 5: | Line 5: | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco), catalyzes the addition of CO2 to ribulose 1,5-bisphosphate in all, photosynthetic organisms. During catalysis, the bisphosphate is depleted, by reactions other than carboxylation and some of the products are potent, inhibitors of rubisco. We have used one of these, xylulose, 1,5-bisphosphate as an analogue of the natural substrate and, co-crystallized it with the enzyme. RESULTS: We have solved the crystal, structure of Synechococcus rubisco with bound xylulose 1,5-bisphosphate to, 2.3 A and compared it with the previously solved 2'-carboxylarabinitol, 1,5-bisphosphate (2CABP) enzyme quaternary complex. Unlike 2CABP, xylulose, 1,5-bisphosphate forms a binary complex with no activating CO2 or, essential metal present. . | + | BACKGROUND: Ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco), catalyzes the addition of CO2 to ribulose 1,5-bisphosphate in all, photosynthetic organisms. During catalysis, the bisphosphate is depleted, by reactions other than carboxylation and some of the products are potent, inhibitors of rubisco. We have used one of these, xylulose, 1,5-bisphosphate as an analogue of the natural substrate and, co-crystallized it with the enzyme. RESULTS: We have solved the crystal, structure of Synechococcus rubisco with bound xylulose 1,5-bisphosphate to, 2.3 A and compared it with the previously solved 2'-carboxylarabinitol, 1,5-bisphosphate (2CABP) enzyme quaternary complex. Unlike 2CABP, xylulose, 1,5-bisphosphate forms a binary complex with no activating CO2 or, essential metal present. Five flexible elements that restrict access to, the active site in the 2CABP complex also close off the active site in the, xylulose 1,5-bisphosphate complex, stabilized by interactions with the, hydrated form of the analogue. CONCLUSIONS: Xylulose 1,5-bisphosphate, induces closure of critical loops of the protein without essential, cofactors resident at the active site. In the case of rubisco in one, species, catalysis is completely inhibited. |
==About this Structure== | ==About this Structure== | ||
| - | 1RSC is a | + | 1RSC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Synechococcus_sp. Synechococcus sp.] with XBP 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] Structure known Active Site: 1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RSC OCA]. |
==Reference== | ==Reference== | ||
| Line 20: | Line 20: | ||
[[Category: lyase (carbon-carbon)]] | [[Category: lyase (carbon-carbon)]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:56:46 2007'' |
Revision as of 12:51, 5 November 2007
|
STRUCTURE OF AN EFFECTOR INDUCED INACTIVATED STATE OF RIBULOSE BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE: THE BINARY COMPLEX BETWEEN ENZYME AND XYLULOSE BISPHOSPHATE
Overview
BACKGROUND: Ribulose 1,5-bisphosphate carboxylase/oxygenase (rubisco), catalyzes the addition of CO2 to ribulose 1,5-bisphosphate in all, photosynthetic organisms. During catalysis, the bisphosphate is depleted, by reactions other than carboxylation and some of the products are potent, inhibitors of rubisco. We have used one of these, xylulose, 1,5-bisphosphate as an analogue of the natural substrate and, co-crystallized it with the enzyme. RESULTS: We have solved the crystal, structure of Synechococcus rubisco with bound xylulose 1,5-bisphosphate to, 2.3 A and compared it with the previously solved 2'-carboxylarabinitol, 1,5-bisphosphate (2CABP) enzyme quaternary complex. Unlike 2CABP, xylulose, 1,5-bisphosphate forms a binary complex with no activating CO2 or, essential metal present. Five flexible elements that restrict access to, the active site in the 2CABP complex also close off the active site in the, xylulose 1,5-bisphosphate complex, stabilized by interactions with the, hydrated form of the analogue. CONCLUSIONS: Xylulose 1,5-bisphosphate, induces closure of critical loops of the protein without essential, cofactors resident at the active site. In the case of rubisco in one, species, catalysis is completely inhibited.
About this Structure
1RSC is a Protein complex structure of sequences from Synechococcus sp. with XBP as ligand. Active as Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 Structure known Active Site: 1. Full crystallographic information is available from OCA.
Reference
Structure of an effector-induced inactivated state of ribulose 1,5-bisphosphate carboxylase/oxygenase: the binary complex between enzyme and xylulose 1,5-bisphosphate., Newman J, Gutteridge S, Structure. 1994 Jun 15;2(6):495-502. PMID:7922027
Page seeded by OCA on Mon Nov 5 14:56:46 2007
