2d3t
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(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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Revision as of 07:18, 21 November 2007
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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 ACO and NAD 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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