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1bwv

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==Overview==
==Overview==
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We determined the crystal structure of spinach ribulose-1, 5-bisphosphate, carboxylase/oxygenase (Rubisco) by x-ray diffraction at 1.8-A resolution, and found that the enzyme contained two kinds of S, SI and SII, present in, equal number and disposed in an orderly way within the Rubisco holoenzyme., The electron density maps suggested that leucine was at residue 56 in SI, although histidine was at that position in SII. There were other residue, differences. Thus, spinach Rubisco has a L8SI4SII4 subunit structure. The, orderly disposition of the heterogeneous small subunits in the Rubisco, holoenzyme provides accounts of a multigene family of S in plants.
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We determined the crystal structure of spinach ribulose-1, 5-bisphosphate carboxylase/oxygenase (Rubisco) by x-ray diffraction at 1.8-A resolution and found that the enzyme contained two kinds of S, SI and SII, present in equal number and disposed in an orderly way within the Rubisco holoenzyme. The electron density maps suggested that leucine was at residue 56 in SI, although histidine was at that position in SII. There were other residue differences. Thus, spinach Rubisco has a L8SI4SII4 subunit structure. The orderly disposition of the heterogeneous small subunits in the Rubisco holoenzyme provides accounts of a multigene family of S in plants.
==About this Structure==
==About this Structure==
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[[Category: lyase]]
[[Category: lyase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:34:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:56 2008''

Revision as of 10:00, 21 February 2008

Image:1bwv.jpg

1bwv, resolution 2.4Å

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ACTIVATED RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE (RUBISCO) COMPLEXED WITH THE REACTION INTERMEDIATE ANALOGUE 2-CARBOXYARABINITOL 1,5-BISPHOSPHATE

Overview

We determined the crystal structure of spinach ribulose-1, 5-bisphosphate carboxylase/oxygenase (Rubisco) by x-ray diffraction at 1.8-A resolution and found that the enzyme contained two kinds of S, SI and SII, present in equal number and disposed in an orderly way within the Rubisco holoenzyme. The electron density maps suggested that leucine was at residue 56 in SI, although histidine was at that position in SII. There were other residue differences. Thus, spinach Rubisco has a L8SI4SII4 subunit structure. The orderly disposition of the heterogeneous small subunits in the Rubisco holoenzyme provides accounts of a multigene family of S in plants.

About this Structure

1BWV is a Protein complex structure of sequences from Galdieria partita with and as ligands. Active as Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.

Reference

Orderly disposition of heterogeneous small subunits in D-ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach., Shibata N, Inoue T, Fukuhara K, Nagara Y, Kitagawa R, Harada S, Kasai N, Uemura K, Kato K, Yokota A, Kai Y, J Biol Chem. 1996 Oct 25;271(43):26449-52. PMID:8900108

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