PDBsum entry 1jr8

Oxidoreductase

PDB id: 1jr8

Contents

Protein chains

105 a.a. *

Ligands

FAD ×2

Waters ×282

* Residue conservation analysis

PDB id:

1jr8

Name:

Oxidoreductase

Title:

Crystal structure of erv2p

Structure:

Erv2 protein, mitochondrial. Chain: a, b. Fragment: protease-resistant domain. Synonym: erv2p sulfhydryl oxidase. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: erv2. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

1.50Å R-factor: 0.208 R-free: 0.233

Authors:

E.Gross,C.S.Sevier,A.Vala,C.A.Kaiser,D.Fass

Key ref:

E.Gross et al. (2002). A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p. Nat Struct Biol, 9, 61-67. PubMed id: 11740506 DOI: 10.1038/nsb740

Date:

13-Aug-01 Release date: 28-Dec-01

Protein chains

Q12284  (ERV2_YEAST) -  FAD-linked sulfhydryl oxidase ERV2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 196 a.a.

Struc: 105 a.a.

Enzyme reactions

• Enzyme class: E.C.1.8.3.2 - thiol oxidase.
• Reaction: 2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1038/nsb740

Nat Struct Biol 9:61-67 (2002)

PubMed id: 11740506

A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p.

E.Gross, C.S.Sevier, A.Vala, C.A.Kaiser, D.Fass.

ABSTRACT

Erv2p is an FAD-dependent sulfhydryl oxidase that can promote disulfide bond formation during protein biosynthesis in the yeast endoplasmic reticulum. The structure of Erv2p, determined by X-ray crystallography to 1.5 A resolution, reveals a helix-rich dimer with no global resemblance to other known FAD-binding proteins or thiol oxidoreductases. Two pairs of cysteine residues are required for Erv2p activity. The first (Cys-Gly-Glu-Cys) is adjacent to the isoalloxazine ring of the FAD. The second (Cys-Gly-Cys) is part of a flexible C-terminal segment that can swing into the vicinity of the first cysteine pair in the opposite subunit of the dimer and may shuttle electrons between substrate protein dithiols and the FAD-proximal disulfide.

Selected figure(s)

Figure 4.
Figure 4. FAD binding site. a, A ribbon diagram of the polypeptide backbone with some side chains and the bound FAD shown in ball-and-stick representation. The bent conformation of the FAD buries the isoalloxazine ring and adenine portions of the cofactor while keeping the intervening regions surface exposed. b, The ribbon trace of the polypeptide backbone has been removed in this panel so that the residues involved in aromatic ring stacking with the FAD can be identified.

Figure 6.
Figure 6. Erv2p flexible C-terminal tail. The four molecules in the asymmetric unit of the crystals grown from the original Erv2- N preparation were superposed to compare the orientations of the C-terminal regions containing the Cys-Gly-Cys sequence. In this crystal, one of the four C-terminal tails packs against the neighboring active site. The arrow indicates the significant conformational differences between the superposed molecules. Shown in the inset is a model of an intersubunit disulfide bond constructed by changing the 1 side chain torsion angles of Cys 178 and Cys 121 to decrease the sulfur -sulfur bond distance between these residues to 2.03 Å.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2002, 9, 61-67) copyright 2002.

Figures were selected by an automated process.