1ok6: Difference between revisions
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[[Image:1ok6.gif|left|200px]]<br /><applet load="1ok6" size=" | [[Image:1ok6.gif|left|200px]]<br /><applet load="1ok6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ok6, resolution 2.40Å" /> | caption="1ok6, resolution 2.40Å" /> | ||
'''ORTHORHOMBIC CRYSTAL FORM OF AN ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE'''<br /> | '''ORTHORHOMBIC CRYSTAL FORM OF AN ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1OK6 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 GOL 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] Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http:// | 1OK6 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 <scene name='pdbligand=GOL:'>GOL</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OK6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: tim barrel]] | [[Category: tim barrel]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:59:11 2008'' | ||
Revision as of 10:59, 3 February 2008
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ORTHORHOMBIC CRYSTAL FORM OF AN ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE
OverviewOverview
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 StructureAbout this Structure
1OK6 is a Single protein structure of sequence from Thermoproteus tenax with as ligand. Active as Fructose-bisphosphate aldolase, with EC number 4.1.2.13 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
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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