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| - | [[Image:1rxo.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1rxo.png|left|200px]] |
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| | {{STRUCTURE_1rxo| PDB=1rxo | SCENE= }} | | {{STRUCTURE_1rxo| PDB=1rxo | SCENE= }} |
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| - | '''ACTIVATED SPINACH RUBISCO IN COMPLEX WITH ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE AND CALCIUM'''
| + | ===ACTIVATED SPINACH RUBISCO IN COMPLEX WITH ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE AND CALCIUM=== |
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| - | ==Overview==
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| - | 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 of the active site by inducing movements of flexible loop regions of the catalytic subunits. In contrast, in the activated complex the active site remains partly open, probably awaiting the binding of the gaseous substrate. By inspection of the structures and by comparison with other complexes of the enzyme we were able to identify a network of hydrogen bonds that stabilise a closed active site structure during crucial steps in the reaction. The present structure underlines the central role of the carbamylated lysine 201 in both activation and catalysis, and completes available structural information for our proposal on the mechanism of the enzyme. | + | The line below this paragraph, {{ABSTRACT_PUBMED_9034362}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9034362 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9034362}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Andersson, I.]] | | [[Category: Andersson, I.]] |
| | [[Category: Taylor, T C.]] | | [[Category: Taylor, T C.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:01:52 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:13:57 2008'' |
Revision as of 10:14, 28 July 2008
Template:STRUCTURE 1rxo
ACTIVATED SPINACH RUBISCO IN COMPLEX WITH ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE AND CALCIUM
Template:ABSTRACT PUBMED 9034362
About this Structure
1RXO is a Protein complex structure of sequences from Spinacia oleracea. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Jul 28 13:13:57 2008
