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Three-dimensional structure of flavocytochrome b2 from baker's yeast at 3.0-A resolution.

Authors
  • Xia, Z X
  • Shamala, N
  • Bethge, P H
  • Lim, L W
  • Bellamy, H D
  • Xuong, N H
  • Lederer, F
  • Mathews, F S
Type
Published Article
Journal
Proceedings of the National Academy of Sciences
Publisher
Proceedings of the National Academy of Sciences
Publication Date
May 01, 1987
Volume
84
Issue
9
Pages
2629–2633
Identifiers
PMID: 3554243
Source
Medline
License
Unknown

Abstract

The structure of flavocytochrome b2 from baker's yeast was solved at 3.0-A resolution by the multiple isomorphous replacement method combined with solvent leveling procedures, using data collected from an area detector. The tetramer of Mr 230,000 has 4-fold symmetry. Each subunit contains a cytochrome domain consisting of the first 100 residues, a flavin-binding domain containing the next 386 residues, and an extended C-terminal tail of 25 residues. The cytochrome domain closely resembles microsomal cytochrome b5, whereas the flavin-binding domain contains a parallel beta 8/alpha 8 barrel motif similar to glycolate oxidase and trimethylamine dehydrogenase. Two of the four cytochrome domains are disordered in the crystals. The flavin ring and heme group are separated by about 16 A between their centers, and their planes are inclined by about 17 degrees to each other.

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