1h1y

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==Overview==
==Overview==
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Cytosolic D-ribulose-5-phosphate 3-epimerase from rice was crystallized, after EDTA treatment and structurally elucidated by X-ray diffraction to, 1.9A resolution. A prominent Zn(2+) site at the active center was, established in a soaking experiment. The structure was compared with that, of the EDTA-treated crystalline enzyme from the chloroplasts of potato, plant leaves showing some structural differences, in particular the, "closed" state of a strongly conserved mobile loop covering the substrate, at its putative binding site. The previous proposal for the active center, was confirmed and the most likely substrate binding position and, conformation was derived from the locations of the bound zinc and sulfate, ions and of three water molecules. Assuming that the bound zinc ion is an, integral part of the enzyme, a reaction mechanism involving a, well-stabilized cis-enediolate intermediate is suggested.
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Cytosolic D-ribulose-5-phosphate 3-epimerase from rice was crystallized after EDTA treatment and structurally elucidated by X-ray diffraction to 1.9A resolution. A prominent Zn(2+) site at the active center was established in a soaking experiment. The structure was compared with that of the EDTA-treated crystalline enzyme from the chloroplasts of potato plant leaves showing some structural differences, in particular the "closed" state of a strongly conserved mobile loop covering the substrate at its putative binding site. The previous proposal for the active center was confirmed and the most likely substrate binding position and conformation was derived from the locations of the bound zinc and sulfate ions and of three water molecules. Assuming that the bound zinc ion is an integral part of the enzyme, a reaction mechanism involving a well-stabilized cis-enediolate intermediate is suggested.
==About this Structure==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Jelakovic, S.]]
[[Category: Jelakovic, S.]]
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[[Category: Schulz, G.E.]]
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[[Category: Schulz, G E.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: 3-epimerase]]
[[Category: 3-epimerase]]
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[[Category: oxidative pentose phosphate pathway]]
[[Category: oxidative pentose phosphate pathway]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:45:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:56:42 2008''

Revision as of 10:56, 21 February 2008


1h1y, resolution 1.87Å

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THE STRUCTURE OF THE CYTOSOLIC D-RIBULOSE-5-PHOSPHATE 3-EPIMERASE FROM RICE COMPLEXED WITH SULFATE

Overview

Cytosolic D-ribulose-5-phosphate 3-epimerase from rice was crystallized after EDTA treatment and structurally elucidated by X-ray diffraction to 1.9A resolution. A prominent Zn(2+) site at the active center was established in a soaking experiment. The structure was compared with that of the EDTA-treated crystalline enzyme from the chloroplasts of potato plant leaves showing some structural differences, in particular the "closed" state of a strongly conserved mobile loop covering the substrate at its putative binding site. The previous proposal for the active center was confirmed and the most likely substrate binding position and conformation was derived from the locations of the bound zinc and sulfate ions and of three water molecules. Assuming that the bound zinc ion is an integral part of the enzyme, a reaction mechanism involving a well-stabilized cis-enediolate intermediate is suggested.

About this Structure

1H1Y is a Single protein structure of sequence from Oryza sativa with as ligand. Active as Ribulose-phosphate 3-epimerase, with EC number 5.1.3.1 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structure and catalytic mechanism of the cytosolic D-ribulose-5-phosphate 3-epimerase from rice., Jelakovic S, Kopriva S, Suss KH, Schulz GE, J Mol Biol. 2003 Feb 7;326(1):127-35. PMID:12547196

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