Structure prediction for the di-heme cytochrome b561 protein family

Denys Bashtovyy, A. Bérczi, Han Asard, T. Páli

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Atomic models possessing the common structural features identified for the cytochrome b561 (cyt b561) protein family are presented. A detailed and extensive sequence analysis was performed in order to identify and characterize protein sequences in this family of transmembrane electron transport proteins. According to transmembrane helix predictions, all sequences contain 6 transmembrane helices of which 2-6 are located closely in the same regions of the 26 sequences in the alignment. A mammalian (Homo sapiens) and a plant (Arabidopsis thaliana) sequence were selected to build 3-dimensional structures at atomic detail using molecular modeling tools. The main structural constraints included the 2 pairs of heme-ligating His residues that are fully conserved in the family and the lipid-facing sides of the helices, which were also very well conserved. The current paper proposes 3-dimensional structures which to our knowledge are the first ones for any protein in the cyt b561 family. The highly conserved His residues anchoring the two hemes on the cytoplasmic side and noncytoplasmic side of the membrane are in all proteins located in the transmembrane helices 2, 4 and 3, 5, respectively. Several highly conserved amino acids with aromatic side chain are identified between the two heme ligation sites. These residues may constitute a putative transmembrane electron transport pathway. The present study demonstrates that the structural features in the cyt b561 family are well conserved at both the sequence and the protein level. The central 4-helix core represents a transmembrane electron transfer architecture that is highly conserved in eukaryotic species.

Original languageEnglish
Pages (from-to)31-40
Number of pages10
JournalProtoplasma
Volume221
Issue number1-2
DOIs
Publication statusPublished - May 2003

Fingerprint

heme
cytochromes
Heme
electron transfer
prediction
Electron Transport
Proteins
transmembrane proteins
proteins
transport proteins
sequence alignment
aromatic compounds
amino acid sequences
sequence analysis
Arabidopsis thaliana
Aromatic Amino Acids
Sequence Alignment
Protein Transport
amino acids
Arabidopsis

Keywords

  • Ascorbic acid
  • Cytochrome b
  • Electron transport
  • Heme protein
  • Protein family
  • Structure prediction

ASJC Scopus subject areas

  • Plant Science
  • Cell Biology

Cite this

Structure prediction for the di-heme cytochrome b561 protein family. / Bashtovyy, Denys; Bérczi, A.; Asard, Han; Páli, T.

In: Protoplasma, Vol. 221, No. 1-2, 05.2003, p. 31-40.

Research output: Contribution to journalArticle

Bashtovyy, Denys ; Bérczi, A. ; Asard, Han ; Páli, T. / Structure prediction for the di-heme cytochrome b561 protein family. In: Protoplasma. 2003 ; Vol. 221, No. 1-2. pp. 31-40.
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