1wdm

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[[Image:1wdm.gif|left|200px]]
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{{STRUCTURE_1wdm| PDB=1wdm | SCENE= }}
{{STRUCTURE_1wdm| PDB=1wdm | SCENE= }}
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'''fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi, form I (native3)'''
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===fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi, form I (native3)===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_15229654}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15229654 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15229654}}
==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/15229654 15229654]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15229654 15229654]
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Reconstitution, morphology and crystallization of a fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi., Ishikawa M, Mikami Y, Usukura J, Iwasaki H, Shinagawa H, Morikawa K, Biochem J. 1997 Dec 15;328 ( Pt 3):815-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9396725 9396725]
[[Category: Acetyl-CoA C-acyltransferase]]
[[Category: Acetyl-CoA C-acyltransferase]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Tsunaka, Y.]]
[[Category: Tsunaka, Y.]]
[[Category: Alpha2beta2 heterotetrameric complex]]
[[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 Jul 28 12:24:06 2008''

Revision as of 09:24, 28 July 2008

Image:1wdm.png

Template:STRUCTURE 1wdm

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

Template:ABSTRACT PUBMED 15229654

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

Reconstitution, morphology and crystallization of a fatty acid beta-oxidation multienzyme complex from Pseudomonas fragi., Ishikawa M, Mikami Y, Usukura J, Iwasaki H, Shinagawa H, Morikawa K, Biochem J. 1997 Dec 15;328 ( Pt 3):815-20. PMID:9396725

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