2wua

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:16, 20 December 2023) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:2wua.jpg|left|200px]]
 
-
<!--
+
==Structure of the peroxisomal 3-ketoacyl-CoA thiolase from Sunflower==
-
The line below this paragraph, containing "STRUCTURE_2wua", creates the "Structure Box" on the page.
+
<StructureSection load='2wua' size='340' side='right'caption='[[2wua]], [[Resolution|resolution]] 1.80&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'>[[2wua]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helianthus_annuus Helianthus annuus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WUA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WUA 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]] 1.8&#8491;</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=2wua FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wua OCA], [https://pdbe.org/2wua PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wua RCSB], [https://www.ebi.ac.uk/pdbsum/2wua PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wua ProSAT]</span></td></tr>
-
{{STRUCTURE_2wua| PDB=2wua | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q6W6X6_HELAN Q6W6X6_HELAN]
 +
== 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/wu/2wua_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2wua ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The breakdown of fatty acids, performed by the beta-oxidation cycle, is crucial for plant germination and sustainability. beta-Oxidation involves four enzymatic reactions. The final step, in which a two-carbon unit is cleaved from the fatty acid, is performed by a 3-ketoacyl-CoA thiolase (KAT). The shortened fatty acid may then pass through the cycle again (until reaching acetoacetyl-CoA) or be directed to a different cellular function. Crystal structures of KAT from Arabidopsis thaliana and Helianthus annuus have been solved to 1.5 and 1.8 A resolution, respectively. Their dimeric structures are very similar and exhibit a typical thiolase-like fold; dimer formation and active site conformation appear in an open, active, reduced state. Using an interdisciplinary approach, we confirmed the potential of plant KATs to be regulated by the redox environment in the peroxisome within a physiological range. In addition, co-immunoprecipitation studies suggest an interaction between KAT and the multifunctional protein that is responsible for the preceding two steps in beta-oxidation, which would allow a route for substrate channeling. We suggest a model for this complex based on the bacterial system.
-
===STRUCTURE OF THE PEROXISOMAL 3-KETOACYL-COA THIOLASE FROM SUNFLOWER===
+
Peroxisomal plant 3-ketoacyl-CoA thiolase structure and activity are regulated by a sensitive redox switch.,Pye VE, Christensen CE, Dyer JH, Arent S, Henriksen A J Biol Chem. 2010 Jul 30;285(31):24078-88. Epub 2010 May 12. PMID:20463027<ref>PMID:20463027</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 2wua" style="background-color:#fffaf0;"></div>
-
==About this Structure==
+
==See Also==
-
2WUA is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Helianthus_annuus Helianthus annuus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WUA OCA].
+
*[[Thiolase 3D structures|Thiolase 3D structures]]
-
[[Category: Acetyl-CoA C-acyltransferase]]
+
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Helianthus annuus]]
[[Category: Helianthus annuus]]
-
[[Category: Arent, S.]]
+
[[Category: Large Structures]]
-
[[Category: Christensen, C E.]]
+
[[Category: Arent S]]
-
[[Category: Dyer, J H.]]
+
[[Category: Christensen CE]]
-
[[Category: Henriksen, A.]]
+
[[Category: Dyer JH]]
-
[[Category: Pye, V E.]]
+
[[Category: Henriksen A]]
-
[[Category: Acyltransferase]]
+
[[Category: Pye VE]]
-
[[Category: Beta oxidation]]
+
-
[[Category: Cysteine oxidation]]
+
-
[[Category: Plant lipid metabolism]]
+
-
[[Category: Transferase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 12 11:13:06 2010''
+

Current revision

Structure of the peroxisomal 3-ketoacyl-CoA thiolase from Sunflower

PDB ID 2wua

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools