2fjk

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[[Image:2fjk.gif|left|200px]]
[[Image:2fjk.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2fjk |SIZE=350|CAPTION= <scene name='initialview01'>2fjk</scene>, resolution 2.2&Aring;
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The line below this paragraph, containing "STRUCTURE_2fjk", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_2fjk| PDB=2fjk | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fjk OCA], [http://www.ebi.ac.uk/pdbsum/2fjk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fjk RCSB]</span>
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}}
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'''Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus'''
'''Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus'''
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[[Category: Lee, J H.]]
[[Category: Lee, J H.]]
[[Category: Rho, S H.]]
[[Category: Rho, S H.]]
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[[Category: beta-alpha-barrel]]
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[[Category: Beta-alpha-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:58:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:03:40 2008''
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Revision as of 00:58, 4 May 2008

Image:2fjk.gif

Template:STRUCTURE 2fjk

Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus


Overview

It was recently established that fructose-1,6-bisphosphate (FBP) aldolase (FBA) and tagatose-1,6-bisphosphate (TBP) aldolase (TBA), two class II aldolases, are highly specific for the diastereoselective synthesis of FBP and TBP from glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP), respectively. In this paper, we report on a FBA from the thermophile Thermus caldophilus GK24 (Tca) that produces both FBP and TBP from C(3) substrates. Moreover, the FBP:TBP ratio could be adjusted by manipulating the concentrations of G3P and DHAP. This is the first native FBA known to show dual diastereoselectivity among the FBAs and TBAs characterized thus far. To explain the behavior of this enzyme, the X-ray crystal structure of the Tca FBA in complex with DHAP was determined at 2.2A resolution. It appears that as a result of alteration of five G3P binding residues, the substrate binding cavity of Tca FBA has a greater volume than those in the Escherichia coli FBA-phosphoglycolohydroxamate (PGH) and TBA-PGH complexes. We suggest that this steric difference underlies the difference in the diastereoselectivities of these class II aldolases.

About this Structure

2FJK is a Single protein structure of sequence from Thermus caldophilus. Full crystallographic information is available from OCA.

Reference

Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus., Lee JH, Bae J, Kim D, Choi Y, Im YJ, Koh S, Kim JS, Kim MK, Kang GB, Hong SI, Lee DS, Eom SH, Biochem Biophys Res Commun. 2006 Sep 1;347(3):616-25. Epub 2006 Jul 5. PMID:16843441 Page seeded by OCA on Sun May 4 03:58:26 2008

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