1iwa
From Proteopedia
(New page: 200px<br /><applet load="1iwa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iwa, resolution 2.60Å" /> '''RUBISCO FROM GALDIER...) |
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| - | [[Image:1iwa.gif|left|200px]]<br /><applet load="1iwa" size=" | + | [[Image:1iwa.gif|left|200px]]<br /><applet load="1iwa" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1iwa, resolution 2.60Å" /> | caption="1iwa, resolution 2.60Å" /> | ||
'''RUBISCO FROM GALDIERIA PARTITA'''<br /> | '''RUBISCO FROM GALDIERIA PARTITA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the | + | Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the reactions of carboxylation and oxygenation of ribulose-1,5-bisphosphate. These reactions require that the active site should be closed by a flexible loop (loop 6) of the large subunit. Rubisco from a red alga, Galdieria partita, has the highest specificity for carboxylation reaction among the Rubiscos hitherto reported. The crystal structure of unactivated Galdieria Rubisco has been determined at 2.6 A resolution. The electron density map reveals that a sulfate binds only to the P1 anion-binding site of the active site and the loop 6 is closed. Galdieria Rubisco has a unique hydrogen bond between the main chain oxygen of Val332 on the loop 6 and the epsilon-amino group of Gln386 of the same large subunit. This interaction is likely to be crucial to understanding for stabilizing the loop 6 in the closed state and to making a higher affinity for anionic ligands. |
==About this Structure== | ==About this Structure== | ||
| - | 1IWA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Galdieria_partita Galdieria partita] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1IWA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Galdieria_partita Galdieria partita] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IWA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: rubisco]] | [[Category: rubisco]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:16:20 2008'' |
Revision as of 11:16, 21 February 2008
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RUBISCO FROM GALDIERIA PARTITA
Overview
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the reactions of carboxylation and oxygenation of ribulose-1,5-bisphosphate. These reactions require that the active site should be closed by a flexible loop (loop 6) of the large subunit. Rubisco from a red alga, Galdieria partita, has the highest specificity for carboxylation reaction among the Rubiscos hitherto reported. The crystal structure of unactivated Galdieria Rubisco has been determined at 2.6 A resolution. The electron density map reveals that a sulfate binds only to the P1 anion-binding site of the active site and the loop 6 is closed. Galdieria Rubisco has a unique hydrogen bond between the main chain oxygen of Val332 on the loop 6 and the epsilon-amino group of Gln386 of the same large subunit. This interaction is likely to be crucial to understanding for stabilizing the loop 6 in the closed state and to making a higher affinity for anionic ligands.
About this Structure
1IWA is a Protein complex structure of sequences from Galdieria partita with as ligand. Active as Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 Full crystallographic information is available from OCA.
Reference
X-ray structure of Galdieria Rubisco complexed with one sulfate ion per active site., Okano Y, Mizohata E, Xie Y, Matsumura H, Sugawara H, Inoue T, Yokota A, Kai Y, FEBS Lett. 2002 Sep 11;527(1-3):33-6. PMID:12220629
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