3U2L

Crystal structure of human ALR mutant C142S.

Summary for 3U2L

• Entry DOI: 10.2210/pdb3u2l/pdb
• Related: 3O55 3U2M
• Descriptor: FAD-linked sulfhydryl oxidase ALR, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: flavoprotein, alr, sulfhydryl oxidase, flavin, fad
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Mitochondrion intermembrane space. Isoform 2: Cytoplasm: P55789
• Total number of polymer chains: 1
• Total formula weight: 14483.78

Authors

Banci, L.,Bertini, I.,Calderone, V.,Cefaro, C.,Ciofi-Baffoni, S.,Gallo, A. (deposition date: 2011-10-04, release date: 2012-06-06, Last modification date: 2024-11-06)

Primary citation

Banci, L.,Bertini, I.,Calderone, V.,Cefaro, C.,Ciofi-Baffoni, S.,Gallo, A.,Tokatlidis, K.
An electron-transfer path through an extended disulfide relay system: the case of the redox protein ALR.
J.Am.Chem.Soc., 134:1442-1445, 2012

PubMed Abstract: The oxidative folding mechanism in the intermembrane space of human mitochondria underpins a disulfide relay system consisting of the import receptor Mia40 and the homodimeric FAD-dependent thiol oxidase ALR. The flavoprotein ALR receives two electrons per subunit from Mia40, which are then donated through one-electron reactions to two cytochrome c molecules, thus mediating a switch from two-electron to one-electron transfer. We dissect here the mechanism of the electron flux within ALR, characterizing at the atomic level the ALR intermediates that allow electrons to rapidly flow to cytochrome c. The intermediate critical for the electron-transfer process implies the formation of a specific inter-subunit disulfide which exclusively allows electron flow from Mia40 to FAD. This finding allows us to present a complete model for the electron-transfer pathway in ALR.

PubMed: 22224850
DOI: 10.1021/ja209881f

Experimental method

X-RAY DIFFRACTION (1.95 Å)