1ok4
From Proteopedia
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==Overview== | ==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 ... | + | 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 bound to dihydroxyacetone phosphate was solved at 2.1-A, resolution. Comparison of the active site residues with those of classical, FBPAs, which share no significant sequence identity but display the same, overall fold, reveals a common ancestry between these two families of, FBPAs. Structural comparisons, furthermore, establish an evolutionary link, to the triosephosphate isomerases, a superfamily hitherto considered, independent from the superfamily of aldolases. |
==About this Structure== | ==About this Structure== | ||
| - | 1OK4 is a | + | 1OK4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax] with 13P as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OK4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:31:23 2007'' |
Revision as of 11:26, 5 November 2007
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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 bound to dihydroxyacetone phosphate was solved at 2.1-A, resolution. Comparison of the active site residues with those of classical, FBPAs, which share no significant sequence identity but display the same, overall fold, reveals a common ancestry between these two families of, FBPAs. Structural comparisons, furthermore, establish an evolutionary link, to the triosephosphate isomerases, a superfamily hitherto considered, independent from the superfamily of aldolases.
About this Structure
1OK4 is a Single protein structure of sequence from Thermoproteus tenax with 13P 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
Page seeded by OCA on Mon Nov 5 13:31:23 2007
