1rcx
From Proteopedia
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| - | [[Image:1rcx.gif|left|200px]] | + | [[Image:1rcx.gif|left|200px]] |
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| - | '''NON-ACTIVATED SPINACH RUBISCO IN COMPLEX WITH ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE''' | + | {{Structure |
| + | |PDB= 1rcx |SIZE=350|CAPTION= <scene name='initialview01'>1rcx</scene>, resolution 2.4Å | ||
| + | |SITE= <scene name='pdbsite=ACB:Active+Site'>ACB</scene>, <scene name='pdbsite=ACE:Active+Site'>ACE</scene>, <scene name='pdbsite=ACH:Active+Site'>ACH</scene>, <scene name='pdbsite=ACK:Active+Site'>ACK</scene>, <scene name='pdbsite=ACL:Active+Site'>ACL</scene>, <scene name='pdbsite=ACO:Active+Site'>ACO</scene>, <scene name='pdbsite=ACR:Active+Site'>ACR</scene> and <scene name='pdbsite=ACV:Active+Site'>ACV</scene> | ||
| + | |LIGAND= <scene name='pdbligand=RUB:RIBULOSE-1,5-DIPHOSPHATE'>RUB</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NON-ACTIVATED SPINACH RUBISCO IN COMPLEX WITH ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RCX is a [ | + | 1RCX is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. The following page contains interesting information on the relation of 1RCX with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb11_1.html Rubisco]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RCX OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9034362 9034362] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ribulose-bisphosphate carboxylase]] | [[Category: Ribulose-bisphosphate carboxylase]] | ||
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[[Category: lyase (carbon-carbon)]] | [[Category: lyase (carbon-carbon)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:49:53 2008'' |
Revision as of 11:49, 20 March 2008
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| , resolution 2.4Å | |||||||
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| Sites: | , , , , , , and | ||||||
| Ligands: | |||||||
| Activity: | Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NON-ACTIVATED SPINACH RUBISCO IN COMPLEX WITH ITS SUBSTRATE RIBULOSE-1,5-BISPHOSPHATE
Overview
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.
About this Structure
1RCX is a Protein complex structure of sequences from Spinacia oleracea. The following page contains interesting information on the relation of 1RCX with [Rubisco]. 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 Thu Mar 20 13:49:53 2008
