1t9g
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1t9g.gif|left|200px]] | [[Image:1t9g.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1t9g", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_1t9g| PDB=1t9g | SCENE= }} | |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''Structure of the human MCAD:ETF complex''' | '''Structure of the human MCAD:ETF complex''' | ||
| Line 35: | Line 32: | ||
[[Category: Thiel, A van.]] | [[Category: Thiel, A van.]] | ||
[[Category: Toogood, H S.]] | [[Category: Toogood, H S.]] | ||
| - | [[Category: | + | [[Category: Electron transfer]] |
| - | [[Category: | + | [[Category: Fatty acid oxidation]] |
| - | [[Category: | + | [[Category: Human electron transferring flavoprotein]] |
| - | [[Category: | + | [[Category: Human medium chain acyl coa dehydrogenase]] |
| - | [[Category: | + | [[Category: Protein:protein complex]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:42:17 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:42, 3 May 2008
Structure of the human MCAD:ETF complex
Contents |
Overview
The crystal structure of the human electron transferring flavoprotein (ETF).medium chain acyl-CoA dehydrogenase (MCAD) complex reveals a dual mode of protein-protein interaction, imparting both specificity and promiscuity in the interaction of ETF with a range of structurally distinct primary dehydrogenases. ETF partitions the functions of partner binding and electron transfer between (i) the recognition loop, which acts as a static anchor at the ETF.MCAD interface, and (ii) the highly mobile redox active FAD domain. Together, these enable the FAD domain of ETF to sample a range of conformations, some compatible with fast interprotein electron transfer. Disorders in amino acid or fatty acid catabolism can be attributed to mutations at the protein-protein interface. Crucially, complex formation triggers mobility of the FAD domain, an induced disorder that contrasts with general models of protein-protein interaction by induced fit mechanisms. The subsequent interfacial motion in the MCAD.ETF complex is the basis for the interaction of ETF with structurally diverse protein partners. Solution studies using ETF and MCAD with mutations at the protein-protein interface support this dynamic model and indicate ionic interactions between MCAD Glu(212) and ETF Arg alpha(249) are likely to transiently stabilize productive conformations of the FAD domain leading to enhanced electron transfer rates between both partners.
Disease
Known disease 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
1T9G is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex., Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D, J Biol Chem. 2004 Jul 30;279(31):32904-12. Epub 2004 May 24. PMID:15159392 Page seeded by OCA on Sat May 3 09:42:17 2008
Categories: Acyl-CoA dehydrogenase | Homo sapiens | Protein complex | Basran, J. | Leys, D. | Scrutton, N S. | Sutcliffe, M J. | Thiel, A van. | Toogood, H S. | Electron transfer | Fatty acid oxidation | Human electron transferring flavoprotein | Human medium chain acyl coa dehydrogenase | Protein:protein complex
