1RSC

STRUCTURE OF AN EFFECTOR INDUCED INACTIVATED STATE OF RIBULOSE BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE: THE BINARY COMPLEX BETWEEN ENZYME AND XYLULOSE BISPHOSPHATE

Summary for 1RSC

• Entry DOI: 10.2210/pdb1rsc/pdb
• Descriptor: RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (LARGE CHAIN), RIBULOSE 1,5 BISPHOSPHATE CARBOXYLASE/OXYGENASE (SMALL CHAIN), XYLULOSE-1,5-BISPHOSPHATE, ... (4 entities in total)
• Functional Keywords: lyase (carbon-carbon)
• Biological source: Synechococcus elongatus; More
• Total number of polymer chains: 16
• Total formula weight: 529415.02

Authors

Newman, J.,Gutteridge, S. (deposition date: 1994-03-29, release date: 1995-05-08, Last modification date: 2024-12-25)

Primary citation

Newman, J.,Gutteridge, S.
Structure of an effector-induced inactivated state of ribulose 1,5-bisphosphate carboxylase/oxygenase: the binary complex between enzyme and xylulose 1,5-bisphosphate.
Structure, 2:495-502, 1994

PubMed Abstract: 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.

PubMed: 7922027
DOI: 10.1016/S0969-2126(00)00050-2

Experimental method

X-RAY DIFFRACTION (2.3 Å)