1ok6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ok6.gif|left|200px]]<br /><applet load="1ok6" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ok6.gif|left|200px]]
-
caption="1ok6, resolution 2.40&Aring;" />
+
 
-
'''ORTHORHOMBIC CRYSTAL FORM OF AN ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE'''<br />
+
{{Structure
 +
|PDB= 1ok6 |SIZE=350|CAPTION= <scene name='initialview01'>1ok6</scene>, resolution 2.40&Aring;
 +
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>
 +
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=
 +
}}
 +
 
 +
'''ORTHORHOMBIC CRYSTAL FORM OF AN ARCHAEAL FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==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 <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].
+
1OK6 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=1OK6 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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12941964 12941964]
+
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]]
Line 31: Line 40:
[[Category: tim barrel]]
[[Category: tim barrel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:18:38 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:11:58 2008''

Revision as of 11:12, 20 March 2008

Image:1ok6.gif


PDB ID 1ok6

Drag the structure with the mouse to rotate
, resolution 2.40Å
Sites:
Ligands:
Activity: Fructose-bisphosphate aldolase, with EC number 4.1.2.13
Coordinates: save as pdb, mmCIF, xml



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 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

1OK6 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

Page seeded by OCA on Thu Mar 20 13:11:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ok6"
Personal tools