2a1u: Difference between revisions
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[[Image:2a1u.gif|left|200px]] | [[Image:2a1u.gif|left|200px]] | ||
'''Crystal structure of the human ETF E165betaA mutant''' | {{Structure | ||
|PDB= 2a1u |SIZE=350|CAPTION= <scene name='initialview01'>2a1u</scene>, resolution 2.11Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=AMP:ADENOSINE MONOPHOSPHATE'>AMP</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of the human ETF E165betaA mutant''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2A1U is a [ | 2A1U 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=2A1U 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: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: mobile domain]] | [[Category: mobile domain]] | ||
''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 15:44:21 2008'' | ||
Revision as of 13:44, 20 March 2008
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| 2a1u, resolution 2.11Å | |||||||||||||
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| Ligands: | FAD and AMP | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal structure of the human ETF E165betaA mutant
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: Glutaricaciduria, type IIA OMIM:[608053], Glutaricaciduria, type IIB OMIM:[130410]
About this Structure
2A1U 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
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