4E0H

Crystal structure of FAD binding domain of Erv1 from Saccharomyces cerevisiae

Summary for 4E0H

• Entry DOI: 10.2210/pdb4e0h/pdb
• Related: 1OQC 4E0I
• Descriptor: Mitochondrial FAD-linked sulfhydryl oxidase ERV1, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: four-helix bundle, flavin-linked sulfhydryl oxidase, fad binding, oxidation, mitochondrial intermembrane space, oxidoreductase
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Mitochondrion intermembrane space: P27882
• Total number of polymer chains: 1
• Total formula weight: 13584.02

Authors

Guo, P.C.,Ma, J.D.,Jiang, Y.L.,Wang, S.J.,Hu, T.T.,Chen, Y.X.,Zhou, C.Z. (deposition date: 2012-03-04, release date: 2012-08-29, Last modification date: 2023-11-08)

Primary citation

Guo, P.C.,Ma, J.D.,Jiang, Y.L.,Wang, S.J.,Bao, Z.Z.,Yu, X.J.,Chen, Y.,Zhou, C.Z.
Structure of yeast sulfhydryl oxidase erv1 reveals electron transfer of the disulfide relay system in the mitochondrial intermembrane space
J.Biol.Chem., 287:34961-34969, 2012

PubMed Abstract: The disulfide relay system in the mitochondrial intermembrane space drives the import of proteins with twin CX(9)C or twin CX(3)C motifs by an oxidative folding mechanism. This process requires disulfide bond transfer from oxidized Mia40 to a substrate protein. Reduced Mia40 is reoxidized/regenerated by the FAD-linked sulfhydryl oxidase Erv1 (EC 1.8.3.2). Full-length Erv1 consists of a flexible N-terminal shuttle domain (NTD) and a conserved C-terminal core domain (CTD). Here, we present crystal structures at 2.0 Å resolution of the CTD and at 3.0 Å resolution of a C30S/C133S double mutant of full-length Erv1 (Erv1FL). Similar to previous homologous structures, the CTD exists as a homodimer, with each subunit consisting of a conserved four-helix bundle that accommodates the isoalloxazine ring of FAD and an additional single-turn helix. The structure of Erv1FL enabled us to identify, for the first time, the three-dimensional structure of the Erv1NTD, which is an amphipathic helix flanked by two flexible loops. This structure also represents an intermediate state of electron transfer from the NTD to the CTD of another subunit. Comparative structural analysis revealed that the four-helix bundle of the CTD forms a wide platform for the electron donor NTD. Moreover, computational simulation combined with multiple-sequence alignment suggested that the amphipathic helix close to the shuttle redox enter is critical for the recognition of Mia40, the upstream electron donor. These findings provide structural insights into electron transfer from Mia40 via the shuttle domain of one subunit of Erv1 to the CTD of another Erv1 subunit.

PubMed: 22910915
DOI: 10.1074/jbc.M112.394759

Experimental method

X-RAY DIFFRACTION (2 Å)