2d3t
From Proteopedia
(New page: 200px<br /><applet load="2d3t" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d3t, resolution 3.4Å" /> '''Fatty Acid beta-oxida...) |
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| - | [[Image:2d3t.gif|left|200px]]<br /><applet load="2d3t" size=" | + | [[Image:2d3t.gif|left|200px]]<br /><applet load="2d3t" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2d3t, resolution 3.4Å" /> | caption="2d3t, resolution 3.4Å" /> | ||
'''Fatty Acid beta-oxidation multienzyme complex from Pseudomonas Fragi, Form V'''<br /> | '''Fatty Acid beta-oxidation multienzyme complex from Pseudomonas Fragi, Form V'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The quaternary structure of a fatty acid beta-oxidation multienzyme | + | The quaternary structure of a fatty acid beta-oxidation multienzyme complex, catalyzing three sequential reactions, was investigated by X-ray crystallographic and small-angle X-ray solution scattering analyses. X-ray crystallography revealed an intermediate structure of the complex among the previously reported structures. However, the theoretical scattering curves calculated from the crystal structures remarkably disagree with the experimental profiles. Instead, an ensemble of the atomic models, which were all calculated by rigid-body optimization, reasonably explained the experimental data. These structures significantly differ from those in the crystals, but they maintain the substrate binding pocket at the domain boundary. Comparisons among these structures indicated that binding of 3-hydroxyhexadecanoyl-CoA or nicotinamide adenine dinucleotide induces domain rearrangements in the complex. The conformational changes suggest the structural events occurring during the chain reaction catalyzed by the multienzyme complex. |
==About this Structure== | ==About this Structure== | ||
| - | 2D3T is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_fragi Pseudomonas fragi] with ACO and NAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 2D3T is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_fragi Pseudomonas fragi] with <scene name='pdbligand=ACO:'>ACO</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D3T OCA]. |
==Reference== | ==Reference== | ||
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[[Category: alpha2beta2 heterotetrameric complex]] | [[Category: alpha2beta2 heterotetrameric complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:05 2008'' |
Revision as of 14:55, 21 February 2008
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Fatty Acid beta-oxidation multienzyme complex from Pseudomonas Fragi, Form V
Overview
The quaternary structure of a fatty acid beta-oxidation multienzyme complex, catalyzing three sequential reactions, was investigated by X-ray crystallographic and small-angle X-ray solution scattering analyses. X-ray crystallography revealed an intermediate structure of the complex among the previously reported structures. However, the theoretical scattering curves calculated from the crystal structures remarkably disagree with the experimental profiles. Instead, an ensemble of the atomic models, which were all calculated by rigid-body optimization, reasonably explained the experimental data. These structures significantly differ from those in the crystals, but they maintain the substrate binding pocket at the domain boundary. Comparisons among these structures indicated that binding of 3-hydroxyhexadecanoyl-CoA or nicotinamide adenine dinucleotide induces domain rearrangements in the complex. The conformational changes suggest the structural events occurring during the chain reaction catalyzed by the multienzyme complex.
About this Structure
2D3T is a Protein complex structure of sequences from Pseudomonas fragi with and as ligands. Active as Acetyl-CoA C-acyltransferase, with EC number 2.3.1.16 Full crystallographic information is available from OCA.
Reference
Ligand-induced domain rearrangement of fatty acid beta-oxidation multienzyme complex., Tsuchiya D, Shimizu N, Ishikawa M, Suzuki Y, Morikawa K, Structure. 2006 Feb;14(2):237-46. PMID:16472743
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