1iwa

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|PDB= 1iwa |SIZE=350|CAPTION= <scene name='initialview01'>1iwa</scene>, resolution 2.60&Aring;
|PDB= 1iwa |SIZE=350|CAPTION= <scene name='initialview01'>1iwa</scene>, resolution 2.60&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1bwv|1BWV]], [[1ej7|1EJ7]], [[1ir1|1IR1]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iwa OCA], [http://www.ebi.ac.uk/pdbsum/1iwa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iwa RCSB]</span>
}}
}}
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[[Category: Xie, Y.]]
[[Category: Xie, Y.]]
[[Category: Yokota, A.]]
[[Category: Yokota, A.]]
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[[Category: SO4]]
 
[[Category: photosynthesis]]
[[Category: photosynthesis]]
[[Category: rubisco]]
[[Category: rubisco]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:55:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:25:31 2008''

Revision as of 18:25, 30 March 2008


PDB ID 1iwa

Drag the structure with the mouse to rotate
, resolution 2.60Å
Ligands:
Activity: Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39
Related: 1BWV, 1EJ7, 1IR1


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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