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2a1t

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[[Image:2a1t.gif|left|200px]]<br /><applet load="2a1t" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2a1t.gif|left|200px]]
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caption="2a1t, resolution 2.80&Aring;" />
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'''Structure of the human MCAD:ETF E165betaA complex'''<br />
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{{Structure
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|PDB= 2a1t |SIZE=350|CAPTION= <scene name='initialview01'>2a1t</scene>, resolution 2.80&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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|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]
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|GENE=
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}}
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'''Structure of the human MCAD:ETF E165betaA complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15975918 15975918]
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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]]
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[[Category: domain dynamics]]
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[[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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:22:45 2008''
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''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


PDB ID 2a1t

Drag the structure with the mouse to rotate
, 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

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