2a1t
From Proteopedia
(New page: 200px<br /> <applet load="2a1t" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a1t, resolution 2.80Å" /> '''Structure of the hu...) |
|||
| Line 1: | Line 1: | ||
| - | [[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== | ||
| Line 11: | Line 10: | ||
==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== | ||
| Line 19: | Line 18: | ||
[[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]] | ||
| Line 30: | Line 29: | ||
[[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'' |
Revision as of 14:22, 21 February 2008
|
Structure of the human MCAD:ETF E165betaA complex
Contents |
Overview
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
Known diseases associated with this structure: Acyl-CoA dehydrogenase, medium chain, deficiency of OMIM:[607008], Glutaricaciduria, type IIA OMIM:[608053], Glutaricaciduria, type IIB OMIM:[130410]
About this Structure
2A1T is a Protein complex structure of sequences from Homo sapiens with and as ligands. Active as Acyl-CoA dehydrogenase, with EC number 1.3.99.3 Full crystallographic information is available from OCA.
Reference
Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein., Toogood HS, van Thiel A, Scrutton NS, Leys D, J Biol Chem. 2005 Aug 26;280(34):30361-6. Epub 2005 Jun 23. PMID:15975918
Page seeded by OCA on Thu Feb 21 16:22:45 2008
