2fjk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (05:12, 17 October 2024) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2fjk.png|left|200px]]
 
-
<!--
+
==Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus==
-
The line below this paragraph, containing "STRUCTURE_2fjk", creates the "Structure Box" on the page.
+
<StructureSection load='2fjk' size='340' side='right'caption='[[2fjk]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<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>
-
or leave the SCENE parameter empty for the default display.
+
</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='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>
-
{{STRUCTURE_2fjk| PDB=2fjk | SCENE= }}
+
<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>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ALF_THECA ALF_THECA]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<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/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2fjk ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== 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.
-
===Crystal structure of Fructose-1,6-Bisphosphate Aldolase in Thermus caldophilus===
+
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<ref>PMID:16843441</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2fjk" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_16843441}}, adds the Publication Abstract to the page
+
*[[Aldolase 3D structures|Aldolase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 16843441 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_16843441}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
2FJK is a 4 chains structure of sequences from [http://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].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:16843441</ref><references group="xtra"/>
+
-
[[Category: Fructose-bisphosphate aldolase]]
+
[[Category: Thermus caldophilus]]
[[Category: Thermus caldophilus]]
-
[[Category: Eom, S H.]]
+
[[Category: Eom SH]]
-
[[Category: Im, Y J.]]
+
[[Category: Im YJ]]
-
[[Category: Kang, G B.]]
+
[[Category: Kang GB]]
-
[[Category: Kim, M K.]]
+
[[Category: Kim M-K]]
-
[[Category: Lee, J H.]]
+
[[Category: Lee JH]]
-
[[Category: Rho, S H.]]
+
[[Category: Rho S-H]]
-
[[Category: Beta-alpha-barrel]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 10:23:40 2009''
+

Current revision

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

PDB ID 2fjk

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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