3O55
Crystal structure of human FAD-linked augmenter of liver regeneration (ALR)
Summary for 3O55
| Entry DOI | 10.2210/pdb3o55/pdb |
| Related | 2HJ3 3MBG |
| Descriptor | Augmenter of liver regeneration, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total) |
| Functional Keywords | flavin, flavoprotein, sulfhydryl oxidase, fad, gfer, alr |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 15777.34 |
| Authors | Banci, L.,Bertini, I.,Calderone, V.,Cefaro, C.,Ciofi-Baffoni, S.,Gallo, A.,Kallergi, E.,Lionaki, E.,Pozidis, C.,Tokatlidis, K. (deposition date: 2010-07-28, release date: 2011-04-13, Last modification date: 2024-11-20) |
| Primary citation | Banci, L.,Bertini, I.,Calderone, V.,Cefaro, C.,Ciofi-Baffoni, S.,Gallo, A.,Kallergi, E.,Lionaki, E.,Pozidis, C.,Tokatlidis, K. Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR. Proc.Natl.Acad.Sci.USA, 108:4811-4816, 2011 Cited by PubMed Abstract: Oxidative protein folding in the mitochondrial intermembrane space requires the transfer of a disulfide bond from MIA40 to the substrate. During this process MIA40 is reduced and regenerated to a functional state through the interaction with the flavin-dependent sulfhydryl oxidase ALR. Here we present the mechanistic basis of ALR-MIA40 interaction at atomic resolution by biochemical and structural analyses of the mitochondrial ALR isoform and its covalent mixed disulfide intermediate with MIA40. This ALR isoform contains a folded FAD-binding domain at the C-terminus and an unstructured, flexible N-terminal domain, weakly and transiently interacting one with the other. A specific region of the N-terminal domain guides the interaction with the MIA40 substrate binding cleft (mimicking the interaction of the substrate itself), without being involved in the import of ALR. The hydrophobicity-driven binding of this region ensures precise protein-protein recognition needed for an efficient electron transfer process. PubMed: 21383138DOI: 10.1073/pnas.1014542108 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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