2a1t
From Proteopedia
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| - | [[Image:2a1t.gif|left|200px]] | + | [[Image:2a1t.gif|left|200px]] |
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| - | '''Structure of the human MCAD:ETF E165betaA complex''' | + | {{Structure |
| + | |PDB= 2a1t |SIZE=350|CAPTION= <scene name='initialview01'>2a1t</scene>, resolution 2.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Structure of the human MCAD:ETF E165betaA complex''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2A1T is a [ | + | 2A1T is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A1T OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15975918 15975918] |
[[Category: Acyl-CoA dehydrogenase]] | [[Category: Acyl-CoA dehydrogenase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: FAD]] | [[Category: FAD]] | ||
[[Category: conformational sampling]] | [[Category: conformational sampling]] | ||
| - | [[Category: domain | + | [[Category: domain dynamic]] |
[[Category: electron transfer]] | [[Category: electron transfer]] | ||
[[Category: fatty acid b-degradation]] | [[Category: fatty acid b-degradation]] | ||
[[Category: protein:protein complex]] | [[Category: protein:protein complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:44:22 2008'' |
Revision as of 13:44, 20 March 2008
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| , resolution 2.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Acyl-CoA dehydrogenase, with EC number 1.3.99.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Mar 20 15:44:22 2008
