1ok4

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(New page: 200px<br /> <applet load="1ok4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ok4, resolution 2.10&Aring;" /> '''ARCHAEAL FRUCTOSE 1...)
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Revision as of 16:20, 29 October 2007

Image:1ok4.gif

1ok4, resolution 2.10Å

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ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE COVALENTLY BOUND TO THE SUBSTRATE DIHYDROXYACETONE PHOSPHATE

Overview

Fructose-1,6-bisphosphate aldolase (FBPA) catalyzes the reversible, cleavage of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and, dihydroxyacetone phosphate in the glycolytic pathway. FBPAs from archaeal, organisms have recently been identified and characterized as a divergent, family of proteins. Here, we report the first crystal structure of an, archaeal FBPA at 1.9-A resolution. The structure of this 280-kDa protein, complex was determined using single wavelength anomalous dispersion, followed by 10-fold non-crystallographic symmetry averaging and refined to, an R-factor of 14.9% (Rfree 17.9%). The protein forms a dimer of, pentamers, consisting of subunits adopting the ubiquitous (betaalpha)8, barrel fold. Additionally, a crystal structure of the archaeal FBPA, covalently ... [(full description)]

About this Structure

1OK4 is a [Single protein] structure of sequence from [Thermoproteus tenax] with 13P as [ligand]. Active as [[1]], with EC number [4.1.2.13]. Full crystallographic information is available from [OCA].

Reference

Crystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteins., Lorentzen E, Pohl E, Zwart P, Stark A, Russell RB, Knura T, Hensel R, Siebers B, J Biol Chem. 2003 Nov 21;278(47):47253-60. Epub 2003 Aug 26. PMID:12941964

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