Solution NMR structures provide first structural coverage of the large protein domain family PF08369 and complementary structural coverage of dark operative protochlorophyllide oxidoreductase complexes

J Struct Funct Genomics. 2013 Sep;14(3):119-26. doi: 10.1007/s10969-013-9159-5. Epub 2013 Aug 21.

Abstract

High-quality NMR structures of the C-terminal domain comprising residues 484-537 of the 537-residue protein Bacterial chlorophyll subunit B (BchB) from Chlorobium tepidum and residues 9-61 of 61-residue Asr4154 from Nostoc sp. (strain PCC 7120) exhibit a mixed α/β fold comprised of three α-helices and a small β-sheet packed against second α-helix. These two proteins share 29% sequence similarity and their structures are globally quite similar. The structures of BchB(484-537) and Asr4154(9-61) are the first representative structures for the large protein family (Pfam) PF08369, a family of unknown function currently containing 610 members in bacteria and eukaryotes. Furthermore, BchB(484-537) complements the structural coverage of the dark-operating protochlorophyllide oxidoreductase.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / ultrastructure
  • Chlorobium / chemistry
  • Chlorophyll Binding Proteins / chemistry
  • Chlorophyll Binding Proteins / ultrastructure*
  • Nostoc / chemistry
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Oxidoreductases / chemistry
  • Oxidoreductases / ultrastructure*
  • Protochlorophyllide / metabolism

Substances

  • Bacterial Proteins
  • Chlorophyll Binding Proteins
  • Protochlorophyllide
  • Oxidoreductases