1h1z
From Proteopedia
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THE STRUCTURE OF THE CYTOSOLIC D-RIBULOSE-5-PHOSPHATE 3-EPIMERASE FROM RICE COMPLEXED WITH SULFATE AND ZINC
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, ... [(full description)]
About this Structure
1H1Z is a [Single protein] structure of sequence from [Oryza sativa] with ZN and SO4 as [ligands]. Active as [[1]], with EC number [5.1.3.1]. 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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