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The structure of a haemopexin-fold protein from cow pea (Vigna unguiculata) suggests functional diversity of haemopexins in plants.
The structure of a haemopexin-fold protein from cow pea (Vigna unguiculata) suggests functional diversity of haemopexins in plants.
- Source :
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Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2011 Feb 01; Vol. 67 (Pt 2), pp. 193-200. Date of Electronic Publication: 2011 Jan 21. - Publication Year :
- 2011
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Abstract
- The haemopexin fold is present in almost all life forms and is utilized for carrying out diverse physiological functions. The structure of CP4, a haemopexin-fold protein from cow pea (Vigna unguiculata), was determined at 2.1 Å resolution. The protein exists as a monomer both in solution and in the crystal. The structure revealed a typical four-bladed β-propeller topology. The protein exhibits 42% sequence similarity to LS-24 from Lathyrus sativus, with substantial differences in the surface-charge distribution and in the oligomeric state. A structure-based sequence analysis of haemopexin-fold proteins of plant and mammalian origin established a sequence signature associated with the haemopexin motif. This signature sequence enabled the identification of other proteins with possible haemopexin-like topology of both plant and animal origin. Although CP4 shares a structural fold with LS-24 and other haemopexins, biochemical studies indicated possible functional differences between CP4 and LS-24. While both of these proteins exhibit spermine-binding potential, CP4 does not bind to haem, unlike LS-24.
- Subjects :
- Amino Acid Motifs
Amino Acid Sequence
Base Sequence
Calibration
Conserved Sequence
Crystallization
Crystallography, X-Ray methods
Dimerization
Heme metabolism
Hemopexin metabolism
Hydrolysis
Hydrophobic and Hydrophilic Interactions
Lathyrus metabolism
Macromolecular Substances chemistry
Macromolecular Substances metabolism
Models, Molecular
Molecular Sequence Data
Molecular Weight
Plant Proteins isolation & purification
Plant Proteins metabolism
Protein Structure, Secondary
Protein Structure, Tertiary
Protein Subunits chemistry
Proteome analysis
Reference Standards
Seeds chemistry
Sequence Analysis, Protein
Sequence Homology, Amino Acid
Spermine metabolism
Fabaceae metabolism
Hemopexin chemistry
Pisum sativum metabolism
Plant Proteins chemistry
Plants metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1744-3091
- Volume :
- 67
- Issue :
- Pt 2
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Publication Type :
- Academic Journal
- Accession number :
- 21301085
- Full Text :
- https://doi.org/10.1107/S1744309110051250