Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolism.

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作者： Gustavo A,Bezerra ^[1] ; William R,Foster ^[1] ; Henry J,Bailey ^[1] ; Kevin G,Hicks ^[2] ; Sven W,Sauer ^[3] ; Bianca,Dimitrov ^[3] ; Thomas J,McCorvie ^[1] ; Jürgen G,Okun ^[3] ; Jared,Rutter ^[2] ; Stefan,Kölker ^[3] ; Wyatt W,Yue ^[1]

作者单位： Structural Genomics Consortium, Nuffield Department of Medicine, University of Oxford, Oxford, OX3 7DQ, United Kingdom. ^[1] Department of Biochemistry, University of Utah School of Medicine, USA. ^[2] Division of Child Neurology and Metabolic Medicine, Centre for Pediatrics and Adolescent Medicine, Clinic I, University Hospital Heidelberg, Germany. ^[3]

关键词 2-oxoacid de-hydrogenase 2-oxoadipate cryo-EM enzyme mechanisms human DHTKD1 lysine catabolism multi-protein complexes thi-amine diphosphate

DOI 10.1107/S205225252000696X

PMID 32695416

发布时间 2024-04-27

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IUCrJ

2020年7卷Pt 4期

693-706页

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Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolism.

IUCrJ

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IUCrJ

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Crystal structure and interaction studies of human DHTKD1 provide insight into a mitochondrial megacomplex in lysine catabolism.

IUCrJ

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IUCrJ

相关期刊

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