2fjk: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: left|200px<br /><applet load="2fjk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fjk, resolution 2.2Å" /> '''Crystal structure of ... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2fjk.gif|left|200px]]<br /><applet load="2fjk" size=" | [[Image:2fjk.gif|left|200px]]<br /><applet load="2fjk" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2fjk, resolution 2.2Å" /> | caption="2fjk, resolution 2.2Å" /> | ||
'''Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus'''<br /> | '''Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus'''<br /> | ||
==Overview== | ==Overview== | ||
It was recently established that fructose-1,6-bisphosphate (FBP) aldolase | 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== | ==About this Structure== | ||
2FJK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_caldophilus Thermus caldophilus] 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] Full crystallographic information is available from [http:// | 2FJK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_caldophilus Thermus caldophilus] with <scene name='pdbligand=13P:'>13P</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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FJK OCA]. | ||
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus caldophilus]] | [[Category: Thermus caldophilus]] | ||
[[Category: Eom, S | [[Category: Eom, S H.]] | ||
[[Category: Im, Y | [[Category: Im, Y J.]] | ||
[[Category: Kang, G | [[Category: Kang, G B.]] | ||
[[Category: Kim, M | [[Category: Kim, M K.]] | ||
[[Category: Lee, J | [[Category: Lee, J H.]] | ||
[[Category: Rho, S | [[Category: Rho, S H.]] | ||
[[Category: 13P]] | [[Category: 13P]] | ||
[[Category: beta-alpha-barrels]] | [[Category: beta-alpha-barrels]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:01 2008'' | ||
