1ok4
From Proteopedia
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| - | [[Image:1ok4.gif|left|200px]] | + | [[Image:1ok4.gif|left|200px]] |
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| - | '''ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE COVALENTLY BOUND TO THE SUBSTRATE DIHYDROXYACETONE PHOSPHATE''' | + | {{Structure |
| + | |PDB= 1ok4 |SIZE=350|CAPTION= <scene name='initialview01'>1ok4</scene>, resolution 2.10Å | ||
| + | |SITE= <scene name='pdbsite=AC1:13p+Binding+Site+For+Chain+J'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE COVALENTLY BOUND TO THE SUBSTRATE DIHYDROXYACETONE PHOSPHATE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OK4 is a [ | + | 1OK4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OK4 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12941964 12941964] |
[[Category: Fructose-bisphosphate aldolase]] | [[Category: Fructose-bisphosphate aldolase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:11:58 2008'' |
Revision as of 11:11, 20 March 2008
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| , resolution 2.10Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Fructose-bisphosphate aldolase, with EC number 4.1.2.13 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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