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1ok6

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[[Category: tim barrel]]
[[Category: tim barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:49:49 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:57:01 2007''

Revision as of 13:52, 30 October 2007

Image:1ok6.gif

1ok6, resolution 2.40Å

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ORTHORHOMBIC CRYSTAL FORM OF AN ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE

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

1OK6 is a [Single protein] structure of sequence from [Thermoproteus tenax] with GOL as [ligand]. Active as [Fructose-bisphosphate aldolase], with EC number [4.1.2.13]. Structure known Active Site: AC1. 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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