1rxo: Difference between revisions
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[[Category: lyase (carbon-carbon)]] | [[Category: lyase (carbon-carbon)]] | ||
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Revision as of 16:59, 30 October 2007
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ACTIVATED SPINACH RUBISCO IN COMPLEX WITH ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE AND CALCIUM
OverviewOverview
The three-dimensional structure of the complex of ribulose, 1,5-bisphosphate carboxylase/oxygenase (rubisco; EC 4.1.1.39) from spinach, with its natural substrate ribulose 1,5-bisphosphate (RuBP) has been, determined both under activating and non-activating conditions by X-ray, crystallography to a resolution of 2.1 A and 2.4 A, respectively. Under, activating conditions, the use of calcium instead of magnesium as the, activator metal ion enabled us to trap the substrate in a stable complex, for crystallographic analysis. Comparison of the structure of the, activated and the non-activated RuBP complexes shows a tighter binding for, the substrate in the non-activated form of the enzyme, in line with, previous solution studies. In the non-activated complex, the substrate, triggers isolation ... [(full description)]
About this StructureAbout this Structure
1RXO is a [Protein complex] structure of sequences from [Spinacia oleracea] with RUB and CA as [ligands]. Active as [Ribulose-bisphosphate carboxylase], with EC number [4.1.1.39]. Structure known Active Sites: ACB, ACE, ACH and ACL. Full crystallographic information is available from [OCA].
ReferenceReference
The structure of the complex between rubisco and its natural substrate ribulose 1,5-bisphosphate., Taylor TC, Andersson I, J Mol Biol. 1997 Jan 31;265(4):432-44. PMID:9034362
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