TAILIEUCHUNG - Báo cáo khoa học: Dynamics driving function ) new insights from electron transferring flavoproteins and partner complexes

Electron transferring flavoproteins (ETFs) are soluble heterodimeric FAD-containing proteins that function primarily as soluble electron carriers between various flavoprotein dehydrogenases. ETF is positioned at a key metabolic branch point, responsible for transferring electrons from up to 10 primary dehydrogenases to the membrane-bound respiratory chain. | IFEBS Journal REVIEW ARTICLE Dynamics driving function - new insights from electron transferring flavoproteins and partner complexes Helen S. Toogood David Leys and Nigel S. Scrutton Manchester Interdisciplinary Biocentre Faculty of Life Sciences University of Manchester UK Keywords acyl-CoA dehydrogenase conformational sampling electron transferring flavoprotein imprinting trimethylamine dehydrogenase Correspondence N. Scrutton Faculty of Life Sciences University of Manchester 131 Princess Street Manchester M1 7DN UK Fax 44 1613065201 Tel 44 1613065152 E-mail Website http Received 10 July 2007 revised 24 August 2007 accepted 14 September 2007 doi Electron transferring flavoproteins ETFs are soluble heterodimeric FADcontaining proteins that function primarily as soluble electron carriers between various flavoprotein dehydrogenases. ETF is positioned at a key metabolic branch point responsible for transferring electrons from up to 10 primary dehydrogenases to the membrane-bound respiratory chain. Clinical mutations of ETF result in the often fatal disease glutaric aciduria type II. Structural and biophysical studies of ETF in complex with partner proteins have shown that ETF partitions the functions of partner binding and electron transfer between a a recognition loop which acts as a static anchor at the ETF-partner interface and b a highly mobile redox-active FAD domain. Together this enables the FAD domain of ETF to sample a range of conformations some compatible with fast interprotein electron transfer. This conformational sampling enables ETF to recognize structurally distinct partners whilst also maintaining a degree of specificity. Complex formation triggers mobility of the FAD domain an induced disorder mechanism contrasting with the more generally accepted models of protein-protein interaction by induced fit mechanisms. We discuss the implications of the highly dynamic

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