1wdm

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[[Image:1wdm.gif|left|200px]]
[[Image:1wdm.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1wdm |SIZE=350|CAPTION= <scene name='initialview01'>1wdm</scene>, resolution 3.8&Aring;
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The line below this paragraph, containing "STRUCTURE_1wdm", 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=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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/Acetyl-CoA_C-acyltransferase Acetyl-CoA C-acyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.16 2.3.1.16] </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_1wdm| PDB=1wdm | SCENE= }}
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|RELATEDENTRY=[[1wdk|1WDK]], [[1wdl|1WDL]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wdm OCA], [http://www.ebi.ac.uk/pdbsum/1wdm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wdm RCSB]</span>
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}}
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'''fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi, form I (native3)'''
'''fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi, form I (native3)'''
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[[Category: Tsuchiya, D.]]
[[Category: Tsuchiya, D.]]
[[Category: Tsunaka, Y.]]
[[Category: Tsunaka, Y.]]
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[[Category: alpha2beta2 heterotetrameric complex]]
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[[Category: Alpha2beta2 heterotetrameric complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:30:36 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:34:47 2008''
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Revision as of 10:30, 3 May 2008

Image:1wdm.gif

Template:STRUCTURE 1wdm

fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi, form I (native3)


Overview

The atomic view of the active site coupling termed channelling is a major subject in molecular biology. We have determined two distinct crystal structures of the bacterial multienzyme complex that catalyzes the last three sequential reactions in the fatty acid beta-oxidation cycle. The alpha2beta2 heterotetrameric structure shows the uneven ring architecture, where all the catalytic centers of 2-enoyl-CoA hydratase (ECH), L-3-hydroxyacyl-CoA dehydrogenase (HACD) and 3-ketoacyl-CoA thiolase (KACT) face a large inner solvent region. The substrate, anchored through the 3'-phosphate ADP moiety, allows the fatty acid tail to pivot from the ECH to HACD active sites, and finally to the KACT active site. Coupling with striking domain rearrangements, the incorporation of the tail into the KACT cavity and the relocation of 3'-phosphate ADP bring the reactive C2-C3 bond to the correct position for cleavage. The alpha-helical linker specific for the multienzyme contributes to the pivoting center formation and the substrate transfer through its deformation. This channelling mechanism could be applied to other beta-oxidation multienzymes, as revealed from the homology model of the human mitochondrial trifunctional enzyme complex.

About this Structure

1WDM is a Protein complex structure of sequences from Pseudomonas fragi. Full crystallographic information is available from OCA.

Reference

Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex., Ishikawa M, Tsuchiya D, Oyama T, Tsunaka Y, Morikawa K, EMBO J. 2004 Jul 21;23(14):2745-54. Epub 2004 Jul 1. PMID:15229654 Page seeded by OCA on Sat May 3 13:30:36 2008

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