3OYO

Crystal structure of hemopexin fold protein CP4 from cow pea

Summary for 3OYO

• Entry DOI: 10.2210/pdb3oyo/pdb
• Descriptor: hemopexin fold protein CP4, CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: hemopexin, seeds, plant protein
• Biological source: Vigna unguiculata (cowpea)
• Total number of polymer chains: 2
• Total formula weight: 49678.48

Authors

Gaur, V.,Chanana, V.,Salunke, D.M. (deposition date: 2010-09-23, release date: 2011-02-09, Last modification date: 2023-11-01)

Primary citation

Gaur, V.,Chanana, V.,Jain, A.,Salunke, D.M.
The structure of a haemopexin-fold protein from cow pea (Vigna unguiculata) suggests functional diversity of haemopexins in plants
Acta Crystallogr.,Sect.F, 67:193-200, 2011

PubMed 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.

PubMed: 21301085
DOI: 10.1107/S1744309110051250

Experimental method

X-RAY DIFFRACTION (2.1 Å)