2fjk

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

2fjk is a 4 chain structure with sequence from Thermus caldophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALF_THECA

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lee JH, Bae J, Kim D, Choi Y, Im YJ, Koh S, Kim JS, Kim MK, Kang GB, Hong SI, Lee DS, Eom SH. Stereoselectivity of fructose-1,6-bisphosphate aldolase in Thermus caldophilus. Biochem Biophys Res Commun. 2006 Sep 1;347(3):616-25. Epub 2006 Jul 5. PMID:16843441 doi:10.1016/j.bbrc.2006.06.139

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fjk"

@@ Line 3: / Line 3: @@
 <StructureSection load='2fjk' size='340' side='right'caption='[[2fjk]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2fjk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermus_caldophilus"_taguchi_et_al._1983 "thermus caldophilus" taguchi et al. 1983]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FJK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FJK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2fjk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_caldophilus Thermus caldophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FJK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FJK FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=13P:1,3-DIHYDROXYACETONEPHOSPHATE'>13P</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fjk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fjk OCA], [https://pdbe.org/2fjk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fjk RCSB], [https://www.ebi.ac.uk/pdbsum/2fjk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fjk ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2fjk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fjk RCSB], [http://www.ebi.ac.uk/pdbsum/2fjk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fjk ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ALF_THECA ALF_THECA]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 14: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fj/2fjk_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Thermus caldophilus taguchi et al. 1983]]
-[[Category: Fructose-bisphosphate aldolase]]
 [[Category: Large Structures]]
-[[Category: Eom, S H]]
+[[Category: Thermus caldophilus]]
-[[Category: Im, Y J]]
+[[Category: Eom SH]]
-[[Category: Kang, G B]]
+[[Category: Im YJ]]
-[[Category: Kim, M K]]
+[[Category: Kang GB]]
-[[Category: Lee, J H]]
+[[Category: Kim M-K]]
-[[Category: Rho, S H]]
+[[Category: Lee JH]]
-[[Category: Beta-alpha-barrel]]
+[[Category: Rho S-H]]
-[[Category: Lyase]]

2fjk

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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