2a1t: Difference between revisions
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New page: left|200px<br /> <applet load="2a1t" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a1t, resolution 2.80Å" /> '''Structure of the hu... |
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[[Image:2a1t.gif|left|200px]]<br /> | [[Image:2a1t.gif|left|200px]]<br /><applet load="2a1t" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2a1t" size=" | |||
caption="2a1t, resolution 2.80Å" /> | caption="2a1t, resolution 2.80Å" /> | ||
'''Structure of the human MCAD:ETF E165betaA complex'''<br /> | '''Structure of the human MCAD:ETF E165betaA complex'''<br /> | ||
==Overview== | ==Overview== | ||
Crystal structures of protein complexes with electron-transferring | Crystal structures of protein complexes with electron-transferring flavoprotein (ETF) have revealed a dual protein-protein interface with one region serving as anchor while the ETF FAD domain samples available space within the complex. We show that mutation of the conserved Glu-165beta in human ETF leads to drastically modulated rates of interprotein electron transfer with both medium chain acyl-CoA dehydrogenase and dimethylglycine dehydrogenase. The crystal structure of free E165betaA ETF is essentially identical to that of wild-type ETF, but the crystal structure of the E165betaA ETF.medium chain acyl-CoA dehydrogenase complex reveals clear electron density for the FAD domain in a position optimal for fast interprotein electron transfer. Based on our observations, we present a dynamic multistate model for conformational sampling that for the wild-type ETF. medium chain acyl-CoA dehydrogenase complex involves random motion between three distinct positions for the ETF FAD domain. ETF Glu-165beta plays a key role in stabilizing positions incompatible with fast interprotein electron transfer, thus ensuring high rates of complex dissociation. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
2A1T is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with AMP and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acyl-CoA_dehydrogenase Acyl-CoA dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.3 1.3.99.3] Full crystallographic information is available from [http:// | 2A1T is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=AMP:'>AMP</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acyl-CoA_dehydrogenase Acyl-CoA dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.3 1.3.99.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A1T OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Leys, D.]] | [[Category: Leys, D.]] | ||
[[Category: Scrutton, N | [[Category: Scrutton, N S.]] | ||
[[Category: Thiel, A | [[Category: Thiel, A Van.]] | ||
[[Category: Toogood, H | [[Category: Toogood, H S.]] | ||
[[Category: AMP]] | [[Category: AMP]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: protein:protein complex]] | [[Category: protein:protein complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:22:45 2008'' | ||
