1bwv
From Proteopedia
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Revision as of 12:53, 30 October 2007
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ACTIVATED RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (RUBISCO) COMPLEXED WITH THE REACTION INTERMEDIATE ANALOGUE 2-CARBOXYARABINITOL 1,5-BISPHOSPHATE
Overview
We determined the crystal structure of spinach ribulose-1, 5-bisphosphate, carboxylase/oxygenase (Rubisco) by x-ray diffraction at 1.8-A resolution, and found that the enzyme contained two kinds of S, SI and SII, present in, equal number and disposed in an orderly way within the Rubisco holoenzyme., The electron density maps suggested that leucine was at residue 56 in SI, although histidine was at that position in SII. There were other residue, differences. Thus, spinach Rubisco has a L8SI4SII4 subunit structure. The, orderly disposition of the heterogeneous small subunits in the Rubisco, holoenzyme provides accounts of a multigene family of S in plants.
About this Structure
1BWV is a [Protein complex] structure of sequences from [Galdieria partita] with MG and CAP as [ligands]. Active as [Ribulose-bisphosphate carboxylase], with EC number [4.1.1.39]. Structure known Active Sites: MGA, MGC, MGE and MGG. Full crystallographic information is available from [OCA].
Reference
Orderly disposition of heterogeneous small subunits in D-ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach., Shibata N, Inoue T, Fukuhara K, Nagara Y, Kitagawa R, Harada S, Kasai N, Uemura K, Kato K, Yokota A, Kai Y, J Biol Chem. 1996 Oct 25;271(43):26449-52. PMID:8900108
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