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PDBsum entry 1jra
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Oxidoreductase
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PDB id
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1jra
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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A new FAD-Binding fold and intersubunit disulfide shuttle in the thiol oxidase erv2p.
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Authors
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E.Gross,
C.S.Sevier,
A.Vala,
C.A.Kaiser,
D.Fass.
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Ref.
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Nat Struct Biol, 2002,
9,
61-67.
[DOI no: ]
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PubMed id
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Abstract
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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.
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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.
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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.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nat Struct Biol
(2002,
9,
61-67)
copyright 2002.
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