1rsc
From Proteopedia
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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. ... [(full description)]
About this Structure
1RSC is a [Protein complex] structure of sequences from [Synechococcus sp.] with XBP as [ligand]. Active as [[1]], with EC number [4.1.1.39]. 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
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