Acta Crystallographica Section D 2004-09-01

Structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 A resolution.

Eric L Wise, Julie Akana, John A Gerlt, Ivan Rayment

Index: Acta Crystallogr. D Biol. Crystallogr. 60(Pt 9) , 1687-90, (2004)

Full Text: HTML

Abstract

The crystal structure of D-ribulose 5-phosphate 3-epimerase (RPE) from the cyanobacterium Synechocystis was determined by X-ray crystallography to 1.6 A resolution. The enzyme, which catalyzes the epimerization of D-ribulose 5-phosphate and D-xylulose 5-phosphate, assembles as a hexamer of (beta/alpha)(8)-barrels in the crystallographic asymmetric unit. The active site is highly similar to those of two previously reported RPEs and provides further evidence for essential catalytic roles for several active-site residues.


Related Compounds

  • D-RIBULOSE-5-...

Related Articles:

Initial characterization of the human central proteome.

2011-01-01

[BMC Syst. Biol. 5 , 17, (2011)]

Complete sequencing and characterization of 21,243 full-length human cDNAs.

2004-01-01

[Nat. Genet. 36 , 40-5, (2004)]

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

2004-10-01

[Genome Res. 14 , 2121-7, (2004)]

The sequence of the human genome.

2001-02-16

[Science 291(5507) , 1304-51, (2001)]

A broad-host-range expression vector series including a Ptac test plasmid and its application in the expression of the dod gene of Serratia marcescens (coding for ribulose-5-phosphate 3-epimerase) in Pseudomonas stutzeri.

2003-05-01

[Biomol. Eng. 17(1) , 11-6, (2000)]

More Articles...